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Information on EC 1.1.1.25 - shikimate dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.25
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.25 shikimate dehydrogenase (NADP+)
IUBMB Comments
NAD+ cannot replace NADP+ . In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase . cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.1.1.25
- 3-dehydroshikimate
- drug development
-
subdural
-
cinnamyl
- dahps
-
5-enolpyruvylshikimate
-
pentafunctional
- 3-dehydroquinase
-
ammonialyase
- analysis
- diagnostics
- food industry
- agriculture
showSynonyms
shikimate dehydrogenase, skdh, sasdh, mtbsdh, shikimate 5-dehydrogenase, hpsdh, mtbsd, shikimate:nadp+ oxidoreductase, hi0607, tgsdh, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-dehydroquinate dehydratase/shikimate dehydrogenase
5-dehydroshikimate reductase
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-
-
-
5-dehydroshikimic reductase
-
-
-
-
ael1
Af2327
AroE
bifunctional dehydroquinate dehydratase-shikimate dehydrogenase
-
cgR_0495
cgR_1677
dehydroquinate dehydratase/shikimate dehydrogenase
dehydroshikimic reductase
-
-
-
-
DHQ-SDH
DHS reductase
-
-
-
-
DQD/SDH
HpSDH
NAD+-dependent enzyme quinate/shikimate dehydrogenase
NADP-dependent shikimate dehydrogenase
Poptr1
qsuD
quinate/shikimate dehydrogenase
rifI
SD
SDH
sdhL
shikimate 5-dehydrogenase
shikimate dehydrogenase
shikimate oxidoreductase
-
-
-
-
shikimate:NADP oxidoreductase
-
-
-
-
shikimate:NADP+ 5-oxidoreductase
-
-
-
-
shikimate:NADP+ oxidoreductase
-
-
-
-
SKDH
tm0346
YdiB
additional information
dehydroquinate dehydratase/shikimate dehydrogenase
-
shikimate 5-dehydrogenase
-
-
-
-
shikimate dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
-
-
-
-
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
conserved residues Asp103 and Lys67 are important for catalysis in all three paralogues, kinetic mechanism of paralogue HI0607 and substrate binding site
-
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
active site structure, reaction and kinetic mechanisms
-
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
active-site base is K92. After the binding of quinate and NAD+, the oxygen of the C3-OH of quinate forms a hydrogen bond to the side chain of the conserved T88 and K92 functions as the active-site base to remove the proton on the C3-OH. Simultaneously,a hydride is transferred from C3 of quinate to NAD+
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
steady-state ordered bi-bi kinetic mechanism. The hydride transferred from NADPH and protons transferred from the solvent in the catalytic cycle are not significantly rate limiting in the overall reaction. Both hydride and proton transfers are concerted, and acid/base chemistry takes place in catalysis and substrate binding
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
the active enzyme for dehydrogenation of shikimate contains a deprotonated K70 residue, a deprotonated D106, and a protonated Y216. The hydride transfer and the deprotonation of the 3-hydroxyl group of shikimate proceed in a concerted manner. K70 functions as a general base and becomes protonated in the dehydrogenation reaction. The proton is then transferred to the bulk solvent via the short proton-conducting wire. D106 plays a critical role in the transfer of the proton to the bulk solvent
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
the pro-R hydrogen of the nicotinamide C4 is 3.35 A from the C3 of shikimate. The catalytic K385 and D423 residues are proximal to the C3-hydroxyl of shikimate, which is deprotonated in the oxidation reaction. The enzyme adopts a concave architecture that places the active sites in a face-to-face arrangement
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shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
catalytic mechanism, residue Lys69 plays a catalytic role and is not involved in substrate binding, overview
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
the enzyme catalysis follows a sequential random mechanism, enzyme catalysis depends on acid-basic amino acids
-
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
steady-state ordered bi-bi kinetic mechanism. The hydride transferred from NADPH and protons transferred from the solvent in the catalytic cycle are not significantly rate limiting in the overall reaction. Both hydride and proton transfers are concerted, and acid/base chemistry takes place in catalysis and substrate binding
-
-
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
the enzyme catalysis follows a sequential random mechanism, enzyme catalysis depends on acid-basic amino acids
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
redox reaction
reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
chorismate biosynthesis from 3-dehydroquinate
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SYSTEMATIC NAME
IUBMB Comments
shikimate:NADP+ 3-oxidoreductase
NAD+ cannot replace NADP+ [3]. In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase [4]. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
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CAS REGISTRY NUMBER
COMMENTARY
9026-87-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-dehydroshikimate + NADH
shikimate + NAD+
-
Substrates: SDH reaction, very low activity with NAD+
Products: -
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r
quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
Substrates: -
Products: -
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?
3-dehydroquinate
3-dehydroshikimate + H2O
-
Substrates: DQD reaction
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r
3-dehydroquinate
3-dehydroshikimate + H2O
-
Substrates: -
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r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
Substrates: fourth enzyme involved in the shikimate pathway
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r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
Substrates: -
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r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
Substrates: fourth enzyme involved in the shikimate pathway
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r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
Substrates: -
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r
3-dehydroshikimate + NADH + H+
shikimate + NAD+
A4QEK4, A4QB65
Substrates: less than 1% of the rate with 3-dehydroquinate
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r
3-dehydroshikimate + NADH + H+
shikimate + NAD+
A4QEK4, A4QB65
Substrates: less than 1% of the rate with 3-dehydroquinate
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r
3-dehydroshikimate + NADP+
gallate + NADPH + H+
Substrates: -
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r
3-dehydroshikimate + NADP+
gallate + NADPH + H+
Substrates: -
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r
3-dehydroshikimate + NADPH
?
-
Substrates: enzyme of shikimic acid biosynthesis
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r
3-dehydroshikimate + NADPH
?
-
Substrates: pathway of biosynthesis of aromatic amino acids
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r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
Substrates: -
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r
3-dehydroshikimate + NADPH
shikimate + NADP+
Substrates: -
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r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
Substrates: -
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r
3-dehydroshikimate + NADPH
shikimate + NADP+
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Substrates: NADH may substitute for NADPH
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r
3-dehydroshikimate + NADPH
shikimate + NADP+
Substrates: -
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?
3-dehydroshikimate + NADPH
shikimate + NADP+
Substrates: -
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?
3-dehydroshikimate + NADPH
shikimate + NADP+
Substrates: -
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?
3-dehydroshikimate + NADPH
shikimate + NADP+
-
Substrates: -
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r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
Substrates: SDH reaction
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r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
Substrates: -
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r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
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Substrates: structure of the enzyme is a compact alpha/beta sandwich with two distinct domains, responsible for binding substrate and NADP cofactor, respectively
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?
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
Substrates: -
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r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
Substrates: -
Products: -
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?
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
Substrates: -
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r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
Substrates: catalytic mechanism, residue Lys69 plays a catalytic role and is not involved in substrate binding
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r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
Substrates: -
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?, r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
Substrates: -
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r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
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r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
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r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: activity of T381 enzyme mutants, not of wild-type enzyme, see also EC 1.1.1.282
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r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: -
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r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
Substrates: activity by only mutant S275G/T318G, not the wild-type enzyme
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r
quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: in contrast to shikimate, quinate may form a hydrogen bond to the NAD+, and the hydroxyl group of a active-site threonine hydrogen bonds to quinate more effectively than shikimate resulting in a lower Michaelis constant and higher catalytic efficiency for quinate
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?
quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: the fourth enzyme in the shikimate pathway
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r
quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: the fourth enzyme in the shikimate pathway
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r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
Substrates: reversible activity of YdiB, no activity with paralogue HI0607
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r
quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: -
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r
quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: -
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r
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
Substrates: -
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?
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
Substrates: -
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?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: -
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: the enzyme is also active with NAD+
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH
-
Substrates: assay at 24°C, pH 9.0
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?
shikimate + NADP+
3-dehydroshikimate + NADPH
-
Substrates: SDH reaction
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
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?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: reversible activity of YdiB and AroE, paralogue HI0607 catalyzes the oxidative reaction with low activity
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: analysis of the 3-dehydroshikimate binding site
Products: analysis of the 3-dehydroshikimate binding site
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: the fourth enzyme in the shikimate pathway
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: the fourth enzyme in the shikimate pathway
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
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r
additional information
?
-
-
Substrates: the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities, metabolic channeling
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?
additional information
?
-
-
Substrates: the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities
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?
additional information
?
-
Substrates: The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
Products: -
Products: -
?
additional information
?
-
Substrates: The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
Products: -
Products: -
?
additional information
?
-
-
Substrates: The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with quinate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with quinate
Products: -
Products: -
?
additional information
?
-
Substrates: usage of recombinant shikimate dehydrogenase as sensor reaction for determination of the cytosolic NADPH/NADP ratio in Saccharomyces cerevisiae, quantitative measurements of physiological variables in the cytosolic compartment by GC-MS/MS, cytosolic NADPH/NADP ratio in batch experiments, method, overview
Products: -
Products: -
?
additional information
?
-
Substrates: product analysis by GC-MS. No or poor quinate dehydrogenase activity
Products: -
Products: -
?
additional information
?
-
Substrates: product analysis by GC-MS. No or poor quinate dehydrogenase activity
Products: -
Products: -
?
additional information
?
-
Substrates: product analysis by GC-MS. No or poor quinate dehydrogenase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: product analysis by GC-MS. No or poor quinate dehydrogenase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with quinate
Products: -
Products: -
?
additional information
?
-
-
Substrates: fourth enzyme in the shikimate biosynthetic pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
Products: -
Products: -
?
additional information
?
-
Substrates: the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
Products: -
Products: -
?
additional information
?
-
Substrates: the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also shows 3-dehydroquinate dehydratase activity, EC 4.2.1.10
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also shows 3-dehydroquinate dehydratase activity, EC 4.2.1.10
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also shows 3-dehydroquinate dehydratase activity, EC 4.2.1.10
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
Products: -
Products: -
?
additional information
?
-
-
Substrates: under saturating conditions, Poptr1 displays strong activity with shikimate but no detectable activity with quinate even at elevated enzyme concentrations. The isozyme shows no quinate hydrolyase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate. Under saturating conditions, Poptr5 displays strong activity with shikimate but no detectable activity with quinate even at elevated enzyme concentrations. The isozyme shows no quinate hydrolyase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the wild-type enzyme PoptrSDH1 is highly shikimate-specific, only the S275G/T318G mutant shows activity with quinate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with quinate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with quinate
Products: -
Products: -
?
additional information
?
-
Substrates: broad extent to which the SDH enzyme superfamily has diversified. 5 evolutionarily distinct SDH homologs in the genome of the common soil-inhabiting bacterium, Pseudomonas putida KT2440
Products: -
Products: -
?
additional information
?
-
Substrates: broad extent to which the SDH enzyme superfamily has diversified. 5 evolutionarily distinct SDH homologs in the genome of the common soil-inhabiting bacterium, Pseudomonas putida KT2440
Products: -
Products: -
?
additional information
?
-
Substrates: analyzing the catalytic activity of SDH, the enzyme produce shikimate from 3-dehydroshikimate (3-DHS) in the presence of NADPH as a cofactor, whereas it forms gallic acid in the presence of NADP+
Products: -
Products: -
?
additional information
?
-
-
Substrates: analyzing the catalytic activity of SDH, the enzyme produce shikimate from 3-dehydroshikimate (3-DHS) in the presence of NADPH as a cofactor, whereas it forms gallic acid in the presence of NADP+
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with quinate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with quinate
Products: -
Products: -
?
additional information
?
-
Substrates: even in the presence of a high concentration of quinate (4 mM), SDH displays no activity using either NADP+ or NAD+ as a cofactor
Products: -
Products: -
?
additional information
?
-
Substrates: the SDH domain from the Toxoplasma gondii is part of the AROM complex. No activity with quinate
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH1 also produces gallate from shikimate with NADP+
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH1 also produces gallate from shikimate with NADP+
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH1 also produces gallate from shikimate with NADP+
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH1 also produces gallate from shikimate with NADP+
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH2 does not produce gallate from shikimate
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH2 does not produce gallate from shikimate
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH2 does not produce gallate from shikimate
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme VvSDH2 does not produce gallate from shikimate
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-dehydroshikimate + NADP+
gallate + NADPH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: -
Products: -
Products: -
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
Substrates: reversible activity of YdiB, no activity with paralogue HI0607
Products: -
Products: -
r
3-dehydroquinate
3-dehydroshikimate + H2O
-
Substrates: -
Products: -
Products: -
r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
Substrates: fourth enzyme involved in the shikimate pathway
Products: -
Products: -
r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
Substrates: fourth enzyme involved in the shikimate pathway
Products: -
Products: -
r
3-dehydroshikimate + NADPH
?
-
Substrates: enzyme of shikimic acid biosynthesis
Products: -
Products: -
r
3-dehydroshikimate + NADPH
?
-
Substrates: pathway of biosynthesis of aromatic amino acids
Products: -
Products: -
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
Substrates: -
Products: -
Products: -
r
3-dehydroshikimate + NADPH
shikimate + NADP+
Substrates: -
Products: -
Products: -
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
Substrates: -
Products: -
Products: -
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
Substrates: -
Products: -
Products: -
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
Substrates: -
Products: -
Products: -
r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
Substrates: -
Products: -
Products: -
r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: the fourth enzyme in the shikimate pathway
Products: -
Products: -
r
quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: the fourth enzyme in the shikimate pathway
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: the enzyme is also active with NAD+
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: reversible activity of YdiB and AroE, paralogue HI0607 catalyzes the oxidative reaction with low activity
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: the fourth enzyme in the shikimate pathway
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: the fourth enzyme in the shikimate pathway
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities, metabolic channeling
Products: -
Products: -
?
additional information
?
-
-
Substrates: fourth enzyme in the shikimate biosynthetic pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
Products: -
Products: -
?
additional information
?
-
Substrates: the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
Products: -
Products: -
?
additional information
?
-
Substrates: the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
turnover number decreases by more than 300fold when NADP+ is used instead of NAD+, regardless of substrate shikimate or quinate
NADP+
-
high affinity for the enzyme, the residues Gly130 and Ala131 are present in the N-terminal of the helix and those make positive electrostatic interactions with the phosphates of NADP cofactor
NADP+
-
specificity of TgSDH for NADP+ is consistent with the presence of the NRTXXR motif identified in the primary sequence of the protein
NADP+
the enzyme shows a clear preference for NADPH/NADP+ over NADH/ NAD+
NADPH
binding site determinatiion and binding mode analysis, AroE contains a Rossmann fold NADPH binding domain
NADPH
enzyme MtbSDH utilizes NADPH in the proS form, binding structure, overview
NADPH
the enzyme shows a clear preference for NADPH/NADP+ over NADH/ NAD+
additional information
-
dinucleotide cofactor binding domain structure is a Rossmann fold
-
additional information
A4QEK4
NADH shows about 2% of the activity with NADPH
-
additional information
NADH shows about 2% of the activity with NADPH
-
additional information
-
NADH shows about 2% of the activity with NADPH
-
additional information
A4QEK4
NADPH shows about 2.5% of the activity with NADPH
-
additional information
NADPH shows about 2.5% of the activity with NADPH
-
additional information
-
NADPH shows about 2.5% of the activity with NADPH
-
additional information
cofactor binding might trigger domain movement
-
additional information
-
the highest enzyme activity is observed with NADP+, and activity drops by 96% when replacing NADP+ with NAD+ for Poptr1
-
additional information
-
for Poptr5, no activity with shikimate is detectable in the presence of NAD+ even with elevated enzyme concentrations
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
paralogue HI0607 is not affected by 5 mM of Zn2+, Ca2+, Mg2+, or Mn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3E)-3-[2-(4-bromophenyl)hydrazinylidene]piperidine-2,4,6-trione
-
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(butane-1,4-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
-
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(ethane-1,2-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
-
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(propane-1,3-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(3-hydroxypropyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(4-hydroxybutyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(5-hydroxypentyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(6-hydroxyhexyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-tri[(tert-butyldimethylsilyl)oxy]cyclohex-1-enecarboxylic acid
-
(4Z)-4-[2-(3-hydroxyphenyl)triazan-1-ylidene]-5-methyl-2-[(piperidin-1-yl)methyl]-2,4-dihydro-3H-pyrazol-3-one
-
1,2,4-triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.023 mg/ml
1,3-benzodioxole-5-carbothioamide
-
the compound shows higher affinity for the shikimate binding site than for the NADP+ binding site, mixed full inhibition mechanism versus shikimate, non-competitive full inhibition mechanism versus NADP+, interaction analysis and enzyme-bound structure, overview. 75% inhibition at 0.4 mM
2,2'-bithiophene-5-carboxylic acid
-
the inhibitor is identified by virtual screeening, 87% inhibition at 0.2 mM, competitive versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4-oxo-4H-1-benzopyran-3-yl 6-deoxy-alpha-L-mannopyranoside
-
2-(3,4-dihydroxyphenyl)ethyl 6-O-[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]-beta-D-glucopyranoside
-
2-([2-([2-([2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl)-1,3-benzothiazol-6-yl]amino)2-oxoethyl]sulfanyl)-N-(2-naphthyl)acetamide
IC50: 0.0029 mM, competitive inhibition with respect to shikimate, noncompetitive to NADP+, potent antibacterial activity
3,3,3-trifluoro-N-(2-nitrophenyl)-2-(trifluoromethyl)propanamide
-
3,5,7-trihydroxy-3'-(4-hydroxy-3-methoxyphenyl)-2'-(hydroxymethyl)-2,3,3',4'-tetrahydro-2'H,4H-[2,6'-bi-1-benzopyran]-4-one
-
3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate
IC50: 0.0039 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+
3-(3,4-dihydroxyphenyl)-2-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]propanoic acid
-
3-(3-fluoropyridin-4-yl)-6-(phenoxymethyl)-1,2,4-triazolo[3,4-b]-1,3,4-thiadiazole
-
-
3-(4-bromophenyl)-6-((2,4-dichlorophenoxy)methyl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0396 mg/ml
3-(4-bromophenyl)-6-((2-methyl-4-chlorophenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0216 mg/ml
3-(4-bromophenyl)-6-((4-chlorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0363 mg/ml
3-(4-bromophenyl)-6-((4-fluorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0795 mg/ml
3-(4-bromophenyl)-6-((4-methoxyphenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0120 mg/ml
3-(4-bromophenyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0586 mg/ml
3-(4-chlorophenyl)-6-((2-naphthyloxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.168 mg/ml
3-(4-chlorophenyl)-6-((4-fluorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 5.052 mg/ml
3-(4-chlorophenyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.00937 mg/ml
3-(4-fluorophenyl)-6-((2-naphthyloxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
-
3-(4-fluorophenyl)-6-((4-methoxyphenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0663 mg/ml
3-(4-hydroxyphenyl)-4-oxo-4H-1-benzopyran-7-yl hexopyranosiduronic acid
-
3-(beta-naphthylmethyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0407 mg/ml
3-hydroxy-4-(methoxycarbonyl)-2,5-dimethylphenyl 3-formyl-2,4-dihydroxy-6-methylbenzoate
-
3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-1,4,5-trihydroxycyclohexane-1-carboxylic acid
-
4-hydroxy-6-methyl-2-oxo-1-(2-phenylethyl)-1,2-dihydropyridine-3-carbaldehyde
-
4-[[(E)-(2-ethoxy-6-methyl-4-oxo-2H-1-benzopyran-3(4H)-ylidene)methyl]amino]-2-hydroxybenzoic acid
-
5-(6-hydroxy-1-benzofuran-2-yl)-2-[(1E)-3-methylbut-1-en-1-yl]benzene-1,3-diol
-
5-[4-(1H-imidazol-2-ylcarbonyl)phenyl]thiophene-2-carboxylic acid
-
the compound shows higher affinity for the shikimate binding site than for the NADP+ binding site, uncompetitive full inhibition versus shikimate and mixed full inhibition versus NADP+, interaction analysis and enzyme-bound structure, overview. 98% inhibition at 0.4 mM
5-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-2,2-dimethyl-1,3-dioxane-4,6-dione
-
6-((2,4-dichlorophenoxy)methyl)-3-(3-fluoropyridin-4-yl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-((4-bromophenoxy)methyl)-3-(4-bromophenyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0144 mg/ml
6-((4-bromophenoxy)methyl)-3-(4-chlorophenyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.00682 mg/ml
6-((4-fluorophenoxy)methyl)-3-(beta-naphthylmethyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0277 mg/ml
6-amino-1,2,3,4-tetrahydronaphthalen-1-one
-
the compound presents a higher affinity for NADP+ binding site than for shikimate binding, mixed partial inhibition mechanism versus NADP+ and mixed full versus shikimate, interaction analysis and enzyme-bound structure, overview. 91% inhibition at 0.4 m
6-hydroxy-2,3-dihydrobenzo[b]furan-3-one
-
the inhibitor is identified by virtual screeening, 99% inhibition at 0.2 mM, mixed-type inhibition versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues
6-hydroxy-7-methyl-1-benzofuran-3(2H)-one
-
mixed partial inhibition mechanism versus NADP+ and shikimate, interaction analysis and enzyme bound structure, overview. 98% inhibition at 0.4 mM
7-hydroxy-2,2,8-trimethyl-2,3-dihydro-4H-chromen-4-one
-
the inhibitor is identified by virtual screeening, 87% inhibition at 0.2 mM, competitive versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues
ajmalicine
-
(19alpha)-16,17-didehydro-19-methyloxayohimban-16-carboxylic acid methyl ester, from Rauwolfia serpentina leaves and roots, interacting residues are Asp131 and Arg130
aurintricarboxylic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
butyl 2-([3-(2-naphthyloxy)4-oxo-2-(trifluoromethyl)4H-chromen-7-yl]oxy)propanoate
IC50: 0.0134 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+, potent antibacterial activity
cardiolipin
lower inhibitry potency, about 25% inhibition at 0.0025 mM
cyclopropyl(5-hydroxy-1-benzofuran-3-yl)methanone
-
32% inhibition at 0.4 mM
diethylenetriamine pentaacetic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
ethyl 5-(1H-pyrazol-3-yl)thiophene-2-carboxylate
-
28% inhibition at 0.4 mM
hydroquinone
lower inhibitry potency, about 25% inhibition at 0.0025 mM
limonin
-
7,16-dioxo-7,16-dideoxylimondiol, from Citrus sp. fruits, interacting residues are Thr75, Thr78, Val71, Gln101, and Pro103
maesaquinone diacetate
IC50: 0.0035 mM, noncompetitive inhibition with respect to shikimate and NADP+
merbromin
lower inhibitry potency, about 25% inhibition at 0.0025 mM
N-[2,2-dimethyl-6-(1-methyldioxidan-1-ium-1-yl)-3,4-dihydro-2H-1-benzopyran-4-yl]-N2-methyl-N2-[(pyridin-2-yl)methyl]glycinamide
-
34% inhibition at 0.4 mM
NADP+
product inhibition, competitive versus NADPH, noncompetitive versus 3-dehydroshikimate
nordihydroguaiaretic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
pyridoxine
lower inhibitry potency, about 25% inhibition at 0.0025 mM
strictamin
-
akuammilan-17-oic acid methyl ester, from Alstonia scholaris leaves, interacting residues are Tyr129, Gln126, and Leu125
[4-(4-methylperhydro-1,4-diazepin-1-yl)phenyl]methanol
-
67% inhibition at 0.4 mM
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid
-
31% inhibition at 0.2 mM
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid
-
31% inhibition at 0.2 mM
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol
-
49% inhibition at 0.2 mM
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol
-
49% inhibition at 0.2 mM
5-(hex-1-yn-1-yl)furan-2-carboxylic acid
-
29% inhibition at 0.2 mM
curcumin
IC50: 0.0154 mM, noncompetitive inhibition with respect to shikimate and NADP+
epicatechin gallate
inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
epigallocatechin gallate
inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
methyl 3-hydroxy-1-benzothiophene-2-carboxylate
-
33% inhibition at 0.2 mM
methyl 3-hydroxy-1-benzothiophene-2-carboxylate
-
33% inhibition at 0.2 mM
p-chloromercuribenzoate
-
biphasic inhibition: first rapid inhibition leading to loss of 70% activity, then within 5 min loss of the remaining 30% activity, inhibition can be partially hindered by thiols and chloride
shikimate
A4QEK4, A4QB65
shikimate synthesis decreases with increasing shikimate concentration. The relative activity halves at about 1.4 mM shikimate; shikimate synthesis decreases with increasing shikimate concentration. The relative activity halves at about 1.4 mM shikimate
shikimate
product inhibition, noncompetitive versus NADPH, competitive versus 3-dehydroshikimate
[2-[2-(dimethylamino)ethoxy]phenyl]methanol
-
45% inhibition at 0.2 mM
additional information
-
ten clinical isolates of Acinetobacter baumannii are used for inhibitor screening. Ajmalicine, strictamin, and limonin exhibit promising binding towards multiple drug targets of Acinetobacter baumannii in comparison with the binding between standard drugs and their targets. The tested isolates exhibit resistance to antibiotics clinafloxacin, imipenem and polymyxin-E, and the herbal preparations (crude extracts) demonstrate a significant antibacterial potential. Docking study and molecular dynamic simulations, model refinement and validation, overview. Acinetobacter baumannii exhibits resistance to a broad range of antibiotics due to the presence of a protective capsule, lipopolysaccharide, AbaR resistance islands, OmpA, efflux pumps, biofilms formation, and other mechanisms. Evaluation of drug targets in Acinetobacter baumannii. The toxicity prediction for ajmalicine (Rauvolfia serpentina) and strictamin (Alstonia scholaris) are predicted to be non-carcinogenic in both mouse and rat models making them potential leads
-
additional information
screening for polyphenolc enzyme inhibitors, overview
-
additional information
-
screening for polyphenolc enzyme inhibitors, overview
-
additional information
A4QEK4
not inhibitory: quinate; not inhibitory: quinate
-
additional information
not inhibitory: quinate; not inhibitory: quinate
-
additional information
-
not inhibitory: quinate; not inhibitory: quinate
-
additional information
synthesis, biological activity and molecular modelling studies of shikimic acid derivatives as inhibitors of the shikimate dehydrogenase enzyme of Escherichia coli, evaluation for in vitro SDH inhibition and antibacterial activity against Escherichia coli, molecular docking studies, overview. All tested compounds are mixed-type inhibitors, diamide derivatives display more inhibitory activity than synthesised monoamides
-
additional information
-
synthesis, biological activity and molecular modelling studies of shikimic acid derivatives as inhibitors of the shikimate dehydrogenase enzyme of Escherichia coli, evaluation for in vitro SDH inhibition and antibacterial activity against Escherichia coli, molecular docking studies, overview. All tested compounds are mixed-type inhibitors, diamide derivatives display more inhibitory activity than synthesised monoamides
-
additional information
antibacterial activity of inhibitors, overview
-
additional information
-
antibacterial activity of inhibitors, overview
-
additional information
integrated virtual screening/molecular docking-based virtual screening, and antibacterial test for identification of enzyme inhibitors, screening of ZINC database. The HpSDH active site prefers to accommodate amphipathic and polar inhibitors that consist of an aromatic core as well as a number of oxygen-rich polar/charged substituents such as hydroxyl, carbonyl, and carboxyl groups. Subpockets 1- and 2-specific inhibitors exhibit a generally higher activity than subpocket 3-specific inhibitors. Molecular dynamics simulations revealed an intense nonbonded network of hydrogen bonds, Pi-Pi stacking, and van der Waals contacts at the tightly packed complex interfaces of active-site subpockets with their cognate inhibitors, conferring strong stability and specificity to these complex systems. Binding energetic analysis demonstrates that the identified potent inhibitors can target their cognate subpockets with an effective selectivity over noncognate ones. Determination of MIC values of the compounds against Helicobacter strains ATCC43504 and ATCC700392, and structural and energetic analysis of subpocket-inhibitor interactions, overview
-
additional information
-
integrated virtual screening/molecular docking-based virtual screening, and antibacterial test for identification of enzyme inhibitors, screening of ZINC database. The HpSDH active site prefers to accommodate amphipathic and polar inhibitors that consist of an aromatic core as well as a number of oxygen-rich polar/charged substituents such as hydroxyl, carbonyl, and carboxyl groups. Subpockets 1- and 2-specific inhibitors exhibit a generally higher activity than subpocket 3-specific inhibitors. Molecular dynamics simulations revealed an intense nonbonded network of hydrogen bonds, Pi-Pi stacking, and van der Waals contacts at the tightly packed complex interfaces of active-site subpockets with their cognate inhibitors, conferring strong stability and specificity to these complex systems. Binding energetic analysis demonstrates that the identified potent inhibitors can target their cognate subpockets with an effective selectivity over noncognate ones. Determination of MIC values of the compounds against Helicobacter strains ATCC43504 and ATCC700392, and structural and energetic analysis of subpocket-inhibitor interactions, overview
-
additional information
-
structure-activity relationship studies on 1,2,4-triazolo[3,4-b][1,3,4]thiadiazoles as inhibitors of shikimate dehydrogenase, 3,6-disubstituted triazolothiadiazoles synthesis, overview. The compounds exhibit cytotoxicity against Vero and Hep-G2 cellss, IC50 and MIC values
-
additional information
simulations of shikimate dehydrogenase from Mycobacterium tuberculosis in complex with 3-dehydroshikimate and NADPH for MtbSDH inhibition strategy, overview. Rational design of hybrid MtbSDH inhibitors able to bind in both the substrate (DHS) and cofactor (NADPH) pockets
-
additional information
-
simulations of shikimate dehydrogenase from Mycobacterium tuberculosis in complex with 3-dehydroshikimate and NADPH for MtbSDH inhibition strategy, overview. Rational design of hybrid MtbSDH inhibitors able to bind in both the substrate (DHS) and cofactor (NADPH) pockets
-
additional information
screening for polyphenolc enzyme inhibitors, overview. No inhibition by gallic acid, epigallocatechin and epicatechin
-
additional information
-
screening for polyphenolc enzyme inhibitors, overview. No inhibition by gallic acid, epigallocatechin and epicatechin
-
additional information
-
structure-based inhibitor design, small-molecule library screening, inhibition mechanism analysis
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzo-thiadiazole-7-carbothioic acid S-methyl ester
-
activates the enzymes of the anthocyanin metabolism, including the shikimate dehydrogenase, and increases the anthocyanin content in strawberries after harvest, with SKDH playing a crucial role
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Injuries, Traumatic
A review of sub acute subdural hematoma (SASDH) with our institutional experience and its management by double barrel technique (DbT): A novel technique.
Dehydration
Differential responses of five cherry tomato varieties to water stress: Changes on phenolic metabolites and related enzymes.
Hypersensitivity, Delayed
The pathogenesis of subacute subdural hematoma: A report of 3 cases and literature review.
Tuberculosis
Cloning and expression of functional shikimate dehydrogenase (EC 1.1.1.25) from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Expression, purification and properties of shikimate dehydrogenase from Mycobacterium tuberculosis.
Tuberculosis
Functional shikimate dehydrogenase from Mycobacterium tuberculosis H37Rv: purification and characterization.
Tuberculosis
Homogeneous recombinant Mycobacterium tuberculosis shikimate dehydrogenase production: an essential step towards target-based drug design.
Tuberculosis
In silico identification of potential inhibitors against shikimate dehydrogenase through virtual screening and toxicity studies for the treatment of tuberculosis.
Tuberculosis
Kinetic and chemical mechanisms of shikimate dehydrogenase from Mycobacterium tuberculosis.
Tuberculosis
Simulations of Shikimate Dehydrogenase from Mycobacterium tuberculosis in Complex with 3-Dehydroshikimate and NADPH Suggest Strategies for MtbSDH Inhibition.
Tuberculosis
Structural studies of shikimate 5-dehydrogenase from Mycobacterium tuberculosis.
Tuberculosis
The conserved Lysine69 residue plays a catalytic role in Mycobacterium tuberculosis shikimate dehydrogenase.
Tuberculosis
Theoretical characterization of the shikimate 5-dehydrogenase reaction from Mycobacterium tuberculosis by hybrid QC/MM simulations and quantum chemical descriptors.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.046
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
0.157
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.287
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADPH
0.322
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH2, DQD activity
0.331
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADPH
0.381
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
0.381
3-dehydroshikimate
pH 6.5, temperature not specified in the publication
0.449
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
0.466
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHd, with NADPH
0.878
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH3, shikimate formation
0.878
3-dehydroshikimate
pH 6.5, temperature not specified in the publication
0.882
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH3, DQD activity
8.83
3-dehydroshikimate
pH 8.5, 30°C, EcDQD/SDH2, shikimate formation
8.83
3-dehydroshikimate
pH 8.5, temperature not specified in the publication
9.44
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
30.6
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
186
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH4
2.351
L-quinate
-
mutant S275G/T318G, pH and temperature not specified in the publication
3.33
L-quinate
pH and temperature not specified in the publication, mutant T381G
4.075
L-quinate
pH and temperature not specified in the publication, mutant S338G/T381G
4.485
L-quinate
pH and temperature not specified in the publication, mutant T381S
5.135
L-quinate
pH and temperature not specified in the publication, mutant T381A
0.572
NAD+
pH 8.8, presence of 2 mM shikimate
1.083
NAD+
pH 8.8, presence of 2 mM quinate
5.4
NAD+
pH 8.8, presence of 2 mM shikimate
5.43
NAD+
pH 8.8, presence of 2 mM shikimate
0.0073
NADP+
pH 8.8, presence of 2 mM shikimate
0.023
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH3
0.038
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH3
0.0415
NADP+
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
0.0415
NADP+
pH 9.0, temperature not specified in the publication
0.0426
NADP+
-
pH not specified in the publication, 25°C, with shikimate
0.046
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with shikimate
0.0538
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH4
0.0565
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
0.0565
NADP+
pH 9.0, temperature not specified in the publication
0.0652
NADP+
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
0.0652
NADP+
pH 9.0, temperature not specified in the publication
0.112
NADP+
pH 8.8, presence of 2 mM shikimate
0.114
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH1
0.115
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with shikimate
0.138
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with shikimate
0.217
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.00438
NADPH
pH 8.5, 30°C, EcDQD/SDH2, shikimate formation
0.00438
NADPH
pH 8.5, temperature not specified in the publication
0.0231
NADPH
pH 6.5, 30°C, EcDQD/SDH3, shikimate formation
0.0495
NADPH
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
0.0495
NADPH
pH 6.5, temperature not specified in the publication
0.249
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with 3-dehydroshikimate
0.267
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with 3-dehydroshikimate
0.27
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with 3-dehydroshikimate
23.1
NADPH
pH 6.5, temperature not specified in the publication
0.783
quinate
pH 8.8, presence of 2 mM NAD+
0.0046
shikimate
pH 8.8, presence of 2 mM NADP+
0.027
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH3
0.0326
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
0.0326
shikimate
pH 9.0, temperature not specified in the publication
0.0375
shikimate
-
pH not specified in the publication, 25°C, with NADP+
0.07
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH1
0.0786
shikimate
pH 8.8, presence of 2 mM NAD+
0.105
shikimate
pH 8.8, presence of 2 mM NADP+
0.12
shikimate
-
pH and temperature not specified in the publication
0.1468
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH4
0.155
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.2
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADP+
0.223
shikimate
-
with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.273
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADP+
0.279
shikimate
-
pH and temperature not specified in the publication
0.321
shikimate
-
with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.351
shikimate
pH 8.8, presence of 2 mM NAD+
0.422
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
0.548
shikimate
pH and temperature not specified in the publication, mutant S338G
0.604
shikimate
pH and temperature not specified in the publication, wild-type enzyme
0.611
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with NADP+
0.882
shikimate
pH and temperature not specified in the publication, mutant S338G/T381G
1.539
shikimate
pH and temperature not specified in the publication, mutant T381S
1.613
shikimate
pH and temperature not specified in the publication, mutant T381G
2.05
shikimate
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
2.05
shikimate
pH 9.0, temperature not specified in the publication
2.512
shikimate
pH and temperature not specified in the publication, mutant T381A
3.64
shikimate
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
3.64
shikimate
pH 9.0, temperature not specified in the publication
4.2
shikimate
pH 8.8, presence of 2 mM NAD+
additional information
additional information
-
kinetic profile of the recombinant AroE, overview
-
additional information
additional information
steady-state kinetics of recombinant AroE
-
additional information
additional information
-
steady-state kinetics of recombinant AroE
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
the enzyme shows Michaelis-Menten kinetics toward both substrates shikimate and NADP+, kinetic analysis, sequential random mechanism, overview
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.046
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHd, with NADPH
0.168
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADPH
0.405
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADPH
2.14
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
2.87
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
3.67
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
8.62
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
30.9
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
47
3-dehydroshikimate
pH 8.5, 30°C, EcDQD/SDH1, shikimate formation
47
3-dehydroshikimate
pH 8.5, temperature not specified in the publication
57.6
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
57.6
3-dehydroshikimate
pH 6.5, temperature not specified in the publication
60.4
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
95.85
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
307
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
307
3-dehydroshikimate
pH 6.5, temperature not specified in the publication
0.062
L-quinate
pH and temperature not specified in the publication, mutant T381S
0.113
L-quinate
pH and temperature not specified in the publication, mutant T381A
6.7
L-quinate
pH and temperature not specified in the publication, mutant S338G/T381G
8.8
L-quinate
pH and temperature not specified in the publication, mutant T381G
6.72
NAD+
pH 8.8, presence of 2 mM shikimate
40.7
NAD+
pH 8.8, presence of 2 mM quinate
61.1
NAD+
pH 8.8, presence of 2 mM shikimate
97.1
NAD+
pH 8.8, presence of 2 mM shikimate
0.006
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with shikimate
0.043
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with shikimate
0.117
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with shikimate
5.3
NADP+
pH 8.8, presence of 2 mM shikimate
19.78
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH3
26.11
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH3
28.89
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH4
30.7
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH1
70.2
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
70.2
NADP+
pH 9.0, temperature not specified in the publication
135
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
135
NADP+
pH 9.0, temperature not specified in the publication
146.2
NADP+
-
pH not specified in the publication, 25°C, with shikimate
239
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH1
261.5
NADP+
pH 8.8, presence of 2 mM shikimate
792
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
792
NADP+
pH 9.0, temperature not specified in the publication
0.049
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with 3-dehydroshikimate
0.052
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with 3-dehydroshikimate
0.202
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with 3-dehydroshikimate
27.6
NADPH
pH 8.5, 30°C, EcDQD/SDH1, shikimate formation
27.6
NADPH
pH 8.5, temperature not specified in the publication
74.1
NADPH
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
74.1
NADPH
pH 6.5, temperature not specified in the publication
389
NADPH
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
389
NADPH
pH 6.5, temperature not specified in the publication
37.7
quinate
pH 8.8, presence of 2 mM NAD+
0.085
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with NADP+
0.107
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADP+
0.153
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADP+
1.99
shikimate
pH 8.8, presence of 2 mM NAD+
5.16
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH3
5.8
shikimate
pH 8.8, presence of 2 mM NADP+
7.56
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
11.72
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
11.8
shikimate
pH and temperature not specified in the publication, mutant T381A
22
shikimate
pH and temperature not specified in the publication, mutant S338G/T381G
24
shikimate
pH and temperature not specified in the publication, mutant T381G
26.12
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH4
31.2
shikimate
pH 8.8, presence of 2 mM NAD+
55.7
shikimate
pH 8.8, presence of 2 mM NAD+
80.7
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
80.7
shikimate
pH 9.0, temperature not specified in the publication
94.55
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH1
135.8
shikimate
-
pH not specified in the publication, 25°C, with NADP+
146
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
146
shikimate
pH 9.0, temperature not specified in the publication
172
shikimate
pH and temperature not specified in the publication, mutant T381S
266.2
shikimate
pH 8.8, presence of 2 mM NADP+
427
shikimate
pH and temperature not specified in the publication, mutant S338G
516
shikimate
pH and temperature not specified in the publication, wild-type enzyme
755
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
755
shikimate
pH 9.0, temperature not specified in the publication
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
0.099
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHd, with NADPH
0.304
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
0.508
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADPH
1.411
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADPH
4.16
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH3, DQD activity
5.32
3-dehydroshikimate
pH 8.5, 30°C, EcDQD/SDH2, shikimate formation
5.32
3-dehydroshikimate
pH 8.5, temperature not specified in the publication
65.6
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH3, shikimate formation
65.6
3-dehydroshikimate
pH 6.5, temperature not specified in the publication
96
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH2, DQD activity
134.5
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
186
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
611
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
805
3-dehydroshikimate
pH 6.5, temperature not specified in the publication
805.8
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
0.014
L-quinate
pH and temperature not specified in the publication, mutant T381S
0.022
L-quinate
pH and temperature not specified in the publication, mutant T381A
1.64
L-quinate
pH and temperature not specified in the publication, mutant S338G/T381G
2.64
L-quinate
pH and temperature not specified in the publication, mutant T381G
0.13
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with shikimate
0.374
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with shikimate
0.848
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with shikimate
262
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH1
537
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH4
680
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH3
862
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH3
1113
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH1
1690
NADP+
pH 9.0, temperature not specified in the publication
1691.6
NADP+
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
2070
NADP+
pH 9.0, temperature not specified in the publication
2070.6
NADP+
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
14000
NADP+
pH 9.0, temperature not specified in the publication
14017.7
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
0.195
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with 3-dehydroshikimate
0.197
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with 3-dehydroshikimate
0.748
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with 3-dehydroshikimate
3207.8
NADPH
pH 6.5, 30°C, EcDQD/SDH3, shikimate formation
3210
NADPH
pH 6.5, temperature not specified in the publication
6300
NADPH
pH 8.5, temperature not specified in the publication
6301.4
NADPH
pH 8.5, 30°C, EcDQD/SDH2, shikimate formation
7858.6
NADPH
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
7860
NADPH
pH 6.5, temperature not specified in the publication
0.139
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with NADP+
0.535
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADP+
0.56
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADP+
4.7
shikimate
pH and temperature not specified in the publication, mutant T381A
14.9
shikimate
pH and temperature not specified in the publication, mutant T381G
18
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
22.17
shikimate
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
22.2
shikimate
pH 9.0, temperature not specified in the publication
24.9
shikimate
pH and temperature not specified in the publication, mutant S338G/T381G
71.2
shikimate
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
71.3
shikimate
pH 9.0, temperature not specified in the publication
76
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
111.8
shikimate
pH and temperature not specified in the publication, mutant T381S
178
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH4
189
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH3
779.2
shikimate
pH and temperature not specified in the publication, mutant S338G
854.3
shikimate
pH and temperature not specified in the publication, wild-type enzyme
1051
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH1
23159.5
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
23200
shikimate
pH 9.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.458
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(butane-1,4-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.416
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(ethane-1,2-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
25°potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.4
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(propane-1,3-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.733
(3R,4S,5R)-3,4,5-trihydroxy-N-(3-hydroxypropyl)cyclohex-1-ene-1-carboxamide
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.717
(3R,4S,5R)-3,4,5-trihydroxy-N-(4-hydroxybutyl)cyclohex-1-ene-1-carboxamide
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.642
(3R,4S,5R)-3,4,5-trihydroxy-N-(5-hydroxypentyl)cyclohex-1-ene-1-carboxamide
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.587
(3R,4S,5R)-3,4,5-trihydroxy-N-(6-hydroxyhexyl)cyclohex-1-ene-1-carboxamide
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.075
1,3-benzodioxole-5-carbothioamide
-
pH 8.0, 25°C, versus shikimate
0.083
5-[4-(1H-imidazol-2-ylcarbonyl)phenyl]thiophene-2-carboxylic acid
-
pH 8.0, 25°C, versus shikimate
0.213
5-[4-(1H-imidazol-2-ylcarbonyl)phenyl]thiophene-2-carboxylic acid
-
pH 8.0, 25°C, versus NADP+
0.046
6-amino-1,2,3,4-tetrahydronaphthalen-1-one
-
pH 8.0, 25°C, versus NADP+
0.101
6-amino-1,2,3,4-tetrahydronaphthalen-1-one
-
pH 8.0, 25°C, versus shikimate
0.0083
[4-(4-methylperhydro-1,4-diazepin-1-yl)phenyl]methanol
-
pH 8.0, 25°C, versus NADP+
0.0103
[4-(4-methylperhydro-1,4-diazepin-1-yl)phenyl]methanol
-
pH 8.0, 25°C, versus shikimate
additional information
additional information
-
kinetic study of the enzyme-inhibitor complexes
-
additional information
additional information
-
inhibition kinetics and mechanisms, molecular dynamics simulation, overview
-
additional information
additional information
inhibition kinetics, determination of MIC values
-
additional information
additional information
-
inhibition kinetics, determination of MIC values
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.652
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(butane-1,4-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
Escherichia coli
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.588
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(ethane-1,2-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
Escherichia coli
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.589
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(propane-1,3-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
Escherichia coli
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.949
(3R,4S,5R)-3,4,5-trihydroxy-N-(3-hydroxypropyl)cyclohex-1-ene-1-carboxamide
Escherichia coli
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.882
(3R,4S,5R)-3,4,5-trihydroxy-N-(4-hydroxybutyl)cyclohex-1-ene-1-carboxamide
Escherichia coli
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.953
(3R,4S,5R)-3,4,5-trihydroxy-N-(5-hydroxypentyl)cyclohex-1-ene-1-carboxamide
Escherichia coli
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.829
(3R,4S,5R)-3,4,5-trihydroxy-N-(6-hydroxyhexyl)cyclohex-1-ene-1-carboxamide
Escherichia coli
potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH
0.0029
2-([2-([2-([2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl)-1,3-benzothiazol-6-yl]amino)2-oxoethyl]sulfanyl)-N-(2-naphthyl)acetamide
Helicobacter pylori
IC50: 0.0029 mM, competitive inhibition with respect to shikimate, noncompetitive to NADP+, potent antibacterial activity
0.0039
3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate
Helicobacter pylori
IC50: 0.0039 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+
0.0134
butyl 2-([3-(2-naphthyloxy)4-oxo-2-(trifluoromethyl)4H-chromen-7-yl]oxy)propanoate
Helicobacter pylori
IC50: 0.0134 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+, potent antibacterial activity
0.0154
curcumin
Helicobacter pylori
IC50: 0.0154 mM, noncompetitive inhibition with respect to shikimate and NADP+
0.0035
maesaquinone diacetate
Helicobacter pylori
IC50: 0.0035 mM, noncompetitive inhibition with respect to shikimate and NADP+
0.002
epicatechin gallate
Arabidopsis thaliana
pH 8.8, 25°C, recombinant enzyme, AroE domain of the DQD-SDH enzyme
0.0021
epigallocatechin gallate
Arabidopsis thaliana
pH 8.8, 25°C, recombinant enzyme, AroE domain of the DQD-SDH enzyme
0.0098
epigallocatechin gallate
Toxoplasma gondii
-
pH 8.8, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
103
-
wild-type enzyme, pH and temperature not specified in the publication
184
732
9.68
recombinant CEN.PK-aroE strain expressing the enzyme from Eschericha coli, pH 7.0, 25°C
additional information
184
-
after treatment with benzo-thiadiaziole-7-carbothioic acid S-methyl ester
additional information
relative activities for 3-dehydrochikimate reduction and shikimate oxidation of purified recombinant isozymes, overview
additional information
-
relative activities for 3-dehydrochikimate reduction and shikimate oxidation of purified recombinant isozymes, overview
additional information
-
during storage at 1°C, SKDH activity increases in all strawberries
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
10.5
7.3
7.5
8.5
8.8
7
shikimate dehydrogenase assay at, 3-dehydroshikimate production
9
shikimate dehydrogenase assay at, gallate production
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
at pH 7.0, the forward reaction catalyzed by Corynebacterium glutamicum SDH proceeds at a rate about 10fold faster than the reverse reaction
8.5 - 10.5
-
pH 8.5: about 50% of activity maximum, pH 10.5: about 90% of activity maximum
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
22
25
30
50
87
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
-
activity range, maximum activity at 65°C, inactivation at 70°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
Uniprot
brenda
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
Uniprot
brenda
trees in Dabrowa Forest District, Pniewy Forest Division, regional directorate of state forests in Poznan, Poland
-
-
brenda
trees grown in a field at the University of Victoria, Victoria, British Columbia, Canada
-
-
brenda
six PgSDH isozymes (PgSDH1, PgSDH3-1/2, PgSDH3a-1/2, and PgSDH4) are identified in pomegranate, 33 pomegranate accessions, including accession UG28, collected from the Havat Hamataim, Israel
UniProt
brenda
three paralogues: YdiB, AroE, and the shikimate dehydrogenase-like HI0607
-
-
brenda
wild-tpe and clinical Mtb strains MDRTB and RDRTB exhibiting resistant profiles to isoniazid and rifampin
-
-
brenda
wild-tpe and clinical Mtb strains MDRTB and RDRTB exhibiting resistant profiles to isoniazid and rifampin
-
-
brenda
trees grown in a field at the University of Victoria, Victoria, British Columbia, Canada
-
-
brenda
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
after harvest, storage at 1°C, SKDH activity increases in all strawberries
brenda
VvSDH isozymes expression is analysed in the main berry tissues (skin, pulp, and seeds) at three development stages (green stage, veraison, and maturity) to determine their spatial and temporal expression patterns, overview
brenda
highest expression level
brenda
the VvSDH3 expression level rises during the green stage. At veraison, its expression drops and stays very low throughout the ripening stage
brenda
VvSDH4 expression is relatively stable during grape development, except for a peak of expression before veraison
brenda
high expression is observed for isozyme VvSDH1 before veraison but its maximum expression level is reached after veraison
brenda
VvSDH2 expression is relatively stable during grape development, except for a peak of expression before veraison
brenda
lowest expression level
brenda
-
determination of the variability in flowering phenology of Scots pine (Pinus sylvestris L.) clones in a seed orchard, genetic structure and genetic markers (13 isozyme loci and 5 chloroplast and 3 nuclear DNA microsatellite loci) among groups of clones that are differentisated by flowering phenology, overview. The frequency of allele 2 at the shikimate dehydrogenase A locus (ShDH A 2) differs significantly between the groups of early- and late-flowering trees and between the groups of intermediate- and late-flowering trees. In addition, a significant difference in the frequencies of the genotype ShDH A 11 is observed between the intermediate- and late-flowering groups, the ShDH A locus might be considered as isoenzymatic marker that differentiates these flowering groups of Scots pine clones
brenda
immature, highest expression level of VvSDH3
brenda
lowest expression level
brenda
highest expression level
brenda
additional information
activities and phenolic contents in different tissues from CsDQD/SDH isozymes a-d, overview
brenda
additional information
-
activities and phenolic contents in different tissues from CsDQD/SDH isozymes a-d, overview
brenda
additional information
Escherichia coli strain PB12.SA22 and the derivatives ydiB- and ydiB+ are evaluated for their ability to produce shikimate (SA), quinate (QA), 3-dehydroshikimate (DHS), and 3-dehydroquinate (DHQ) in batch culture fermentations growing in 1-l fermentors using 500 ml of a mineral broth supplemented with 25 g/l glucose and 15 g/l YE. Biomass and glucose consumption and the production of aromatic intermediates of the SA pathway, SA, QA, DHQ, and DHS are determined for all derivatives, overview. The highest production of DHQ and DHS is 0.07 and 0.074 g/l, respectively. SA and QA are produced during the early exponential stage, as these compounds are detected during the first 5 h of cultivation (SA = 0.49 g/l and QA = 0.38 g/l, respectively). In the stationary stage and until 20 h of cultivation, this strain consumes the remaining residual glucose. From this time until the end of fermentation, the supernatant concentration of detected SA shows no significant changes, reaching 8.2 g/l by the end of fermentation (50 h), whereas the final QA concentration is 1.52 g/l
brenda
additional information
-
Escherichia coli strain PB12.SA22 and the derivatives ydiB- and ydiB+ are evaluated for their ability to produce shikimate (SA), quinate (QA), 3-dehydroshikimate (DHS), and 3-dehydroquinate (DHQ) in batch culture fermentations growing in 1-l fermentors using 500 ml of a mineral broth supplemented with 25 g/l glucose and 15 g/l YE. Biomass and glucose consumption and the production of aromatic intermediates of the SA pathway, SA, QA, DHQ, and DHS are determined for all derivatives, overview. The highest production of DHQ and DHS is 0.07 and 0.074 g/l, respectively. SA and QA are produced during the early exponential stage, as these compounds are detected during the first 5 h of cultivation (SA = 0.49 g/l and QA = 0.38 g/l, respectively). In the stationary stage and until 20 h of cultivation, this strain consumes the remaining residual glucose. From this time until the end of fermentation, the supernatant concentration of detected SA shows no significant changes, reaching 8.2 g/l by the end of fermentation (50 h), whereas the final QA concentration is 1.52 g/l
-
brenda
additional information
comparison of EcDQD/SDH, UGT84A25a/b, and UGT84A26a/b expression patterns in Eucalyptus camaldulensis, relative EcDQD/SDH mRNA levels in the leaves, stems, and roots are plotted against the relative UGT84A25a/b and UGT84A26a/b mRNA levels in the same samples, and determination of concentrations of the metabolites in the different tissues, overview
brenda
additional information
comparison of EcDQD/SDH, UGT84A25a/b, and UGT84A26a/b expression patterns in Eucalyptus camaldulensis, relative EcDQD/SDH mRNA levels in the leaves, stems, and roots are plotted against the relative UGT84A25a/b and UGT84A26a/b mRNA levels in the same samples, and determination of concentrations of the metabolites in the different tissues, overview
brenda
additional information
comparison of EcDQD/SDH, UGT84A25a/b, and UGT84A26a/b expression patterns in Eucalyptus camaldulensis, relative EcDQD/SDH mRNA levels in the leaves, stems, and roots are plotted against the relative UGT84A25a/b and UGT84A26a/b mRNA levels in the same samples, and determination of concentrations of the metabolites in the different tissues, overview
brenda
additional information
-
comparison of EcDQD/SDH, UGT84A25a/b, and UGT84A26a/b expression patterns in Eucalyptus camaldulensis, relative EcDQD/SDH mRNA levels in the leaves, stems, and roots are plotted against the relative UGT84A25a/b and UGT84A26a/b mRNA levels in the same samples, and determination of concentrations of the metabolites in the different tissues, overview
brenda
additional information
-
poplar DQD/SDHs have distinct expression profiles, organ-specific expression of poplar DQD/SDHs, overview
brenda
additional information
-
poplar DQD/SDHs have distinct expression profiles, organ-specific expression of poplar DQD/SDHs, overview
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid. Best recombinant protein expression protocol of the K69A mutant in insoluble form is using Escherichia coli C41(DE3) strain, grown at 37°C for 24 h after induction with 1 mM IPTG, and cell disruption by sonication. Solubilization of recombinant wild-type and K69A enzymes in inclusion bodies is achieved by either treating the pellet with the denaturant agent urea (3 or 6 M) or by treating with the non ionic detergent zwittergent 3-14 (5%)
-
brenda
DHD/SHD-1 containing a plastidic targeting sequence
brenda
isozyme VvSDH3 contains a putative chloroplastic transit peptide
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
a three-dimensional structural model of TgSDH predicts a high level of conservation in the core structure of the enzyme
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
-
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
-
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
-
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
-
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
-
members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays prove that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity, cf. EC 1.1.1.282
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH3 belongs to group III, group members share about 85% sequence identity, four of them from different species (VvSDH3, CasSDH2, FvSDH1, and EgSDH3) accumulate gallic acid-based tannins
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH4 belongs to group IV, and clusters with with Poptr5, a DQD/SDH characterized in Populus trichocarpa, group members share about 77% sequence identity
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH1 belongs to group I, and clusters with four characterized DQD/SDHs: AtSDH, Poptr1, JrSDH, and NtSDH1, group members share about 75% sequence identity
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH2 belongs to group II, and clusters with Poptr2 and Poptr3, two characterized DQD/SDHs, and NtSDH2, group members share about 71% sequence identity
evolution
plant SDH enzymes are fused to dehydroquinate dehydratases (DQDs, EC 4.2.1.10) to form bifunctional DQD/SDH enzymes. The DQD activity is observed for EcDQD/SDH1, 2, and 3, but not for EcDQD/SDH4a. Among the active enzymes, EcDQD/SDH1 exhibits the highest DQD activity, followed by EcDQD/SDH2 (about 50% of the EcDQD/SDH1 activity) and EcDQD/SDH3 (about 5% of the EcDQD/SDH1 activity). For shikimate formation from 3-DHS as well as shikimate oxidation to 3-DHS, measurable catalytic activities are detected for EcDQD/SDH1-3, but the activities of EcDQD/SDH2 and 3 are less than 20% of those of EcDQD/SDH1. Regarding the cofactor, EcDQD/SDH1-3 have a clear preference for NADPH/NADP+ over NADH/ NAD+. In contrast, EcDQD/SDH4a and b lack shikimate formation activity. For the reverse reaction, the conversion of shikimate to 3-DHS, EcDQD/SDH4a and b display low enzymatic activity with a preference for NAD+ as the cofactor. Both EcDQD/SDH2 and 3 exhibit relatively high gallate formation activity, in contrast to the low activity of EcDQD/SDH1. The preferred cofactor in this reaction is NADP+
evolution
Escherichia coli constitutively expresses two shikimate dehydrogenase paralogues, AroE and the NAD+ -dependent enzyme quinate/shikimate dehydrogenase (YdiB), sharing 25% sequence identity. While AroE is NADP+-dependent, YdiB uses NADP+ or NAD+. Contrary to AroE, YdiB displays a clear activity on quinate, with either NADP+ or NAD+ as a cofactor in addition to shikimate
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
plant QDHs arose directly from bifunctional dehydroquinate dehydratase-shikimate dehydrogenases (DHQD-SDHs) through different convergent evolutionary events, detailed phylogenetic analysis, overview. Eudicot and conifer QDHs arose early in vascular plant evolution whereas Brassicaceae QDHs emerged late, process of recurrent evolution of QDH. This family of proteins independently evolved NAD+ and NADP+ specificity in eudicots. The acquisition of QDH activity by these proteins is accompanied by the inactivation or functional evolution of the DHQD domain, as verified by enzyme activity assays and as reflected in the loss of key DHQD active site residues
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
four CsDQD/SDH isozyme proteins are cloned from Camellia sinensis. Three CsDQD/SDH isozymes show 3-dehydroshikimate (3-DHS) reduction and shikimate (SA) oxidation functions with individual differences between the catalytic efficiency of 3-DHS reduction and SA oxidation. Isozyme CsDQD/SDHa has higher catalytic efficiency for 3-DHS reduction than for SA oxidation, isozyme CsDQD/SDHd shows the opposite tendency, and isozyme CsDQD/SDHc has almost equal catalytic efficiency for 3-DHS reduction and SA oxidation. In vitro, Gallic acid (GA) is mainly generated from 3-DHS through nonenzymatic conversion. Isozymes CsDQD/SDHc and CsDQD/ SDHd genes are involved in GA synthesis
evolution
-
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
-
evolution
-
Escherichia coli constitutively expresses two shikimate dehydrogenase paralogues, AroE and the NAD+ -dependent enzyme quinate/shikimate dehydrogenase (YdiB), sharing 25% sequence identity. While AroE is NADP+-dependent, YdiB uses NADP+ or NAD+. Contrary to AroE, YdiB displays a clear activity on quinate, with either NADP+ or NAD+ as a cofactor in addition to shikimate
-
evolution
-
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
-
evolution
-
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
-
evolution
-
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
-
evolution
-
members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays prove that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity, cf. EC 1.1.1.282
-
malfunction
a contact with the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Arabidopsis thaliana DHQ-SDH causes a substantial reduction in turnover rate
malfunction
in the ydiB knockout mutant, QA production is 6.17% relative to SA (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce QA production below 10% (mol/mol) relative to SA in culture fermentations for SA production. The inactivation of ydiB in Escherichia coli strain PB12.SA22 and the reduction in QA production support the role of YdiB in the synthesis of this compound from DHQ. In the absence of YdiB, the DHS concentration detected in supernatant cultures is maintained relatively constant during the stationary phase
malfunction
-
mutation of Lys69 to alanine significantly reduces the catalytic efficiency of Helicobacter pylori SDH. Mutation of Lys69 triggers the movement of shikimate away from the active site of SDH, thereby disrupting the catalytic activity
malfunction
the mutation of residues Ser338 and NRT to Gly and DI/LD in the SDH unit is the reason for the low activity of isozyme CsDQD/SDHb for 3-DHS reduction and SA oxidation
malfunction
-
in the ydiB knockout mutant, QA production is 6.17% relative to SA (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce QA production below 10% (mol/mol) relative to SA in culture fermentations for SA production. The inactivation of ydiB in Escherichia coli strain PB12.SA22 and the reduction in QA production support the role of YdiB in the synthesis of this compound from DHQ. In the absence of YdiB, the DHS concentration detected in supernatant cultures is maintained relatively constant during the stationary phase
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metabolism
aroE-encoded shikimate dehydrogenase catalyzes the forth reaction in the shikimate pathway
metabolism
-
SKDH is one of the crucial enzymes in the biosynthesis of anthocyanin metabolites, overview
metabolism
-
the enzyme is part of the AROM complex, a large pentafunctional polypeptide, which catalyzes steps two through six of the shikimate pathway in fungi. This complex has the following functional domains (from N- to C-terminus): dehydroquinate synthase, 5-enolypyruvylshikimate-3-phosphate synthase, shikimate kinase, dehydroquinate dehydratase, and SDH. These domains catalyze steps 2, 6, 5, 3, and 4 of the pathway, respectively. The first and last enzymes of the fungal shikimate pathway,3-deoxy-D-arabinoheptulosonate 7-phosphate synthase and chorismate synthase, are discrete enzymes
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites. SDH is part of the Arom complex, that catalyzes both the third and fourth reactions in the shikimate pathway. This large enzyme complex contains five functional domains that are equivalent to the monofunctional enzymes (in bacteria) catalyzing reactions two through six of the shikimate pathway
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
the shikimate pathway leads to the biosynthesis of aromatic amino acids essential for protein biosynthesis and the production of a wide array of plant secondary metabolites. 3-Dehydroquinate is the substrate for shikimate biosynthesis through the sequential actions of dehydroquinate dehydratase (DQD) and shikimate dehydrogenase (SDH) contained in a single protein in plants. Reactions comprising the shikimate/quinate cycle, overview
metabolism
the enzyme catalyze the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
in plants, the shikimate pathway provides aromatic amino acids that are used to generate numerous secondary metabolites, including phenolic compounds. In this pathway, shikimate dehydrogenases catalyse the reversible dehydrogenation of 3-dehydroshikimate to shikimate. Gallic acid metabolism in grape berry tissues along development, overview
metabolism
in plants, the shikimate pathway provides aromatic amino acids that are used to generate numerous secondary metabolites, including phenolic compounds. In this pathway, shikimate dehydrogenases catalyse the reversible dehydrogenation of 3-dehydroshikimate to shikimate
metabolism
in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway, (B) the quinate pathway, (C) the aminoshikimate pathway, overview
metabolism
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in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway. (B) the quinate pathway. (C) the aminoshikimate pathway, overview
metabolism
shikimate, quinate, and gallate biosynthesis catalyzed by DQD/SDH family enzymes, overview. Plant DQD/SDHs are proposed to link the shikimate pathway to gallate and quinate metabolism. Isozymes EcDQD/SDH2 and 3 from Eucalyptus camaldulensis catalyze the NADP+-dependent oxidation of 3-dehydroshikimate to produce gallate. In Eucalyptus camaldulensis, EcDQD/SDH2 and 3 are co-expressed with UGT84A25a/b and UGT84A26a/b involved in hydrolyzable tannin biosynthesis, they catalyze the synthesis of beta-glucogallin
metabolism
shikimate, quinate, and gallate biosynthesis catalyzed by DQD/SDH family enzymes, overview. Plant DQD/SDHs are proposed to link the shikimate pathway to gallate and quinate metabolism. Isozymes EcDQD/SDH2 and 3 from Eucalyptus camaldulensis catalyze the NADP+-dependent oxidation of 3-dehydroshikimate to produce gallate. In Eucalyptus camaldulensis, EcDQD/SDH2 and 3 are co-expressed with UGT84A25a/b and UGT84A26a/b involved in hydrolyzable tannin biosynthesis, catalyze the synthesis of beta-glucogallin
metabolism
shikimate, quinate, and gallate biosynthesis catalyzed by DQD/SDH family enzymes, overview. Plant DQD/SDHs are proposed to link the shikimate pathway to gallate and quinate metabolism
metabolism
shikimate dehydrogenase (HpSDH) is a key enzyme in the shikimate pathway of Helicobacter pylori, which catalyzes the NADPH-dependent reversible reduction of 3-dehydroshikimate to shikimate
metabolism
the enzyme is active in the shikimic acid pathway, which is present in bacteria, fungi, plants and in certain apicomplexan parasites but is absent from humans, pathway overview
metabolism
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link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
-
shikimate dehydrogenase is one of the enzymes involved in the initial steps of the biosynthesis of amino acids such as histidine, tryptophan, tyrosine, phenylalanine, lysine, and aspartic acid
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
the outer peels of Punica granatum fruits possess two groups of polyphenols: anthocyanins (ATs) and hydrolysable tannins (HTs). Their biosynthesis intersects at 3-dehydroshikimate (3-DHS) in the shikimate pathway by the activity of shikimate dehydrogenase (SDH), which converts 3-DHS to shikimate (providing the precursor for AT biosynthesis) or to gallic acid (the precursor for HTs biosynthesis) using NADPH or NADP+ as a cofactor. The outer fruit peel is subjected to light/dark treatment and osmotic stresses (imposed by different sucrose concentrations) showing that light with high sucrose promotes the synthesis of ATs, while dark at the same sucrose concentration promotes the synthesis of HTs. Role of PgSDH in the branch point leading to gallic acid and shikimate, detailed overview. The activity of isozymes PgSDH3, PgSDH3a and PgSDH4 may lead to the synthesis of phenols required for protecting the cells from osmotic stress. Since PgSDH3.2 has a plastid transit peptide, it may mainly use the NADP+ that accumulates in the dark in plastids, while PgSDH3.1, PgSDH3a and PgSDH4 use this cofactor that mainly accumulates during stress
metabolism
3-dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH) is a key enzyme for catalyzing the conversion of 3-dehydroshikimate (3-DHS) to shikimate (SA). It also potentially participates in gallic acid (GA) synthesis in a branch of the SA pathway. Gallic acid (GA) is a precursor for polyphenol synthesis. The CsDQD/SDHc and CsDQD/ SDHd genes are involved in GA synthesis. In plants, DQD/SDH, a bifunctional enzyme, is crucial in the third and fourth reversible reactions in the SA pathway. Biosynthetic pathway of gallic acid and shikimic acid in plants, overview. GA could be spontaneously generated from 3-DHS in the enzymatic or nonenzymatic CsDQD/SDHs assay when using 3-DHS and the coenzyme NADP+ as substrates
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites. SDH is part of the Arom complex, that catalyzes both the third and fourth reactions in the shikimate pathway. This large enzyme complex contains five functional domains that are equivalent to the monofunctional enzymes (in bacteria) catalyzing reactions two through six of the shikimate pathway
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metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
-
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
-
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
-
metabolism
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the shikimate pathway leads to the biosynthesis of aromatic amino acids essential for protein biosynthesis and the production of a wide array of plant secondary metabolites. 3-Dehydroquinate is the substrate for shikimate biosynthesis through the sequential actions of dehydroquinate dehydratase (DQD) and shikimate dehydrogenase (SDH) contained in a single protein in plants. Reactions comprising the shikimate/quinate cycle, overview
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physiological function
A4QEK4, A4QB65
a strain deficient in isoform qsuD does not grow on either shikimate or quinate as sole carbon sources but grows largely unhindered on glucose
physiological function
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Toxoplasma gondii encodes a large pentafunctional polypeptide known as the AROM complex which catalyzes five reactions in the shikimate pathway, a metabolic pathway required for the biosynthesis of the aromatic amino acids and a promising target for anti-parasitic agents. The shikimate dehydrogenase domain (TgSDH) from the Toxoplasma gondii AROM complex catalyzes the NADP+-dependent oxidation of shikimate in the absence of the remaining AROM domains
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes, the enzyme reaction represents the fourth step of the shikimate pathway
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
-
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
-
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
-
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
-
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
-
the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and EC 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
-
the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and E.C. 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
physiological function
the tree species Eucalyptus camaldulensis shows exceptionally high tolerance against aluminum, a widespread toxic metal in acidic soils. In the roots of Eucalyptus camaldulensis, aluminum is detoxified via the complexation with oenothein B, a hydrolyzable tannin. The biosynthesis of oenothein B involves dehydroquinate dehydratase/shikimate dehydrogenases (EcDQD/SDHs) which catalyzes the formation of gallate, the phenolic constituent of hydrolyzable tannins. Two enzymes, EcDQD/SDH2 and 3, in Eucalyptus camaldulensis catalyze the NADP+-dependent oxidation of 3-dehydroshikimate to produce gallate. EcDQD/SDH2 and 3 maintain DQD and SDH activities, resulting in a 3-dehydroshikimate supply for gallate formation
physiological function
the tree species Eucalyptus camaldulensis shows exceptionally high tolerance against aluminum, a widespread toxic metal in acidic soils. In the roots of Eucalyptus camaldulensis, aluminum is detoxified via the complexation with oenothein B, a hydrolyzable tannin. The biosynthesis of oenothein B involves dehydroquinate dehydratase/shikimate dehydrogenases (EcDQD/SDHs) which catalyzes the formation of gallate, the phenolic constituent of hydrolyzable tannins
physiological function
shikimate dehydrogenase (SDH) from Mycobacterium tuberculosis (MtbSDH), encoded by the aroE gene, is essential for viability of Mycobacterium tuberculosis
physiological function
role of shikimate dehydrogenase in controlling the production of anthocyanins (ATs) and hydrolysable tannins (HTs) in the outer peels of pomegranate, Punica granatum. The biosynthesis of HTs and ATs competes for the same substrate, 3-DHS, and that SDH activity is regulated not only by the NADPH/NADP+ ratio, but also by the expression of the PgSDHs
physiological function
-
shikimate dehydrogenase (SDH) catalyzes the reversible, NADPH-dependent reduction of 3-dehydroshikimate to shikimate, involved in the shikimate pathway
physiological function
3-dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH) is a key enzyme for catalyzing the conversion of 3-dehydroshikimate (3-DHS) to shikimate (SA). It also potentially participates in gallic acid (GA) synthesis in a branch of the SA pathway. Quantitative RT-PCR analysis shows that CsDQD/SDHc and CsDQD/SDHd expression is correlated with GA and 1-O-galloyl-beta-D-glucose accumulation in Camellia sinensis. The SA pathway is important to plant growth, development, and defense. Polyphenols in tea plants, including phenolic acids, catechins, and flavonol derivatives, not only determine the mouthfeel of tea infusions but also provide health benefits
physiological function
-
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
-
physiological function
-
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
-
physiological function
-
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
-
physiological function
-
a strain deficient in isoform qsuD does not grow on either shikimate or quinate as sole carbon sources but grows largely unhindered on glucose
-
physiological function
-
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
-
physiological function
-
the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and EC 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
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additional information
the shikimate pathway is an attractive target for the development of antitubercular agents because it is essential in Mycobacterium tuberculosis, the causative agent of tuberculosis, but absent in humans
additional information
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the shikimate pathway is an attractive target for the development of antitubercular agents because it is essential in Mycobacterium tuberculosis, the causative agent of tuberculosis, but absent in humans
additional information
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three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
additional information
modelling of steady state and dynamic fluxes into pentose phosphate pathway and the flux split ratio into glycolysis and pentose phosphate pathway in Saccharomyces recombinantly expressing Escherichia coli shikimate dehydrogenase, overview
additional information
in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQ-SDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQ-SDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processe. Crystallization of the Arabidopsis thaliana protein with shikimate bound in the SDH domain and tartrate (a component of the crystallization solution) in the DHQ domain reveals a V-shaped orientation of the domains. Addition of NADP+ to DHQSDH crystals already containing shikimate in the SDH domain results in the production of 3-dehydroshikimate by the SDH domain and the transfer of the compound to the DHQ active sites
additional information
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in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQSDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQSDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processes
additional information
EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
-
EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
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EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
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EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
analysis of the catalytic active site in the crystal structure of HpSDH in complex with its substrate NADPH and product shikimate. The site can be divided into three spatially separated subpockets that separately correspond to the binding regions of shikimate, NADPH dihydronicotinamide moiety, and NADPH adenine moiety
additional information
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analysis of the catalytic active site in the crystal structure of HpSDH in complex with its substrate NADPH and product shikimate. The site can be divided into three spatially separated subpockets that separately correspond to the binding regions of shikimate, NADPH dihydronicotinamide moiety, and NADPH adenine moiety
additional information
molecular docking calculations and molecular dynamics (MD) simulations for enzyme-substrate interaction and binding structure analysis, model of DHS/NADPH/MtbSDH ternary complex, wild-type and mutant enzymes, detailed overview. Lys69 plays a dual role, in positioning NADPH and in catalysis. Asp105 plays a crucial role in positioning both the epsilon-amino group of Lys69 and nicotinamide ring of NADPH for MtbSDH catalysis but makes no direct contribution to DHS binding. Ala213 is the selection key for NADPH binding with the nicotinamide ring in the proS, rather than proR, conformation in the MtbSDH complex. Residues Ser18, Thr65, Lys69, Gln243, and Gln247 forming hydrogen bonds to 3-dehydroshikimate (DHS)
additional information
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molecular docking calculations and molecular dynamics (MD) simulations for enzyme-substrate interaction and binding structure analysis, model of DHS/NADPH/MtbSDH ternary complex, wild-type and mutant enzymes, detailed overview. Lys69 plays a dual role, in positioning NADPH and in catalysis. Asp105 plays a crucial role in positioning both the epsilon-amino group of Lys69 and nicotinamide ring of NADPH for MtbSDH catalysis but makes no direct contribution to DHS binding. Ala213 is the selection key for NADPH binding with the nicotinamide ring in the proS, rather than proR, conformation in the MtbSDH complex. Residues Ser18, Thr65, Lys69, Gln243, and Gln247 forming hydrogen bonds to 3-dehydroshikimate (DHS)
additional information
only four amino acid residues likely to contribute to specificity for one substrate instead of the other, namely S336, S338, T381 and Y550, all of which would be in the direct vicinity of the quinate C1-hydroxyl. Amino acid S336 has previously been shown by mutational analysis to be critical for shikimate binding. The size of the amino acid side chain at position 381 is a key determinant of substrate specificity
additional information
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three-dimensional stucture homology modelling (PMDB ID PM0080741), model refinement and validation, overview
additional information
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the conserved Lys69 plays an important role in the catalytic activity of Helicobacter pylori SDH, structure-function analysis using the structure of SDH in complex with shikimate and NADP+ (PDB ID 3PHI). Two-layered ONIOM-based quantum mechanics/molecular mechanics (QM/MM) calculation and molecular dynamics (MD) simulations are performed to explore the role of Lys69 in SDH activity, overview. In addition to act as a catalytic base, the conserved Lys69 plays an additional, important role in the maintenance of the substrate shikimate in the active site, facilitating the catalytic reaction between the cofactor NADP+ and shikimate. Shikimate forms hydrogen bonds with Ser16, Ser18, and Tyr210. The C3-hydroxyl group of shikimate is hydrogen bonded to the side chain amide group of Gln237. The C4-hydroxyl group of shikimate donates hydrogen bonds with both the side chain amide group of Asn90 and the carboxylate group of Asp105. The C5-hydroxyl group of shikimate makes hydrogen bonds with the side chain hydroxyl group of Thr65 and the side chain ammonium group of Lys69. Comparison of active site structures of wild-type and mutant K69A enzymes
additional information
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three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
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UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
27076
1 * 27000, recombinant AroE, SDS-PAGE, 1 * 27076, recombinant AroE, mass spectrometry
30000
31000
31010
32000
45000
-
gel filtration, 2 different isoenzymes with molecular weight about 45000 Da
57000
60000
27000
1 * 27000, recombinant AroE, SDS-PAGE, 1 * 27076, recombinant AroE, mass spectrometry
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
monomer
1 * 27000, recombinant AroE, SDS-PAGE, 1 * 27076, recombinant AroE, mass spectrometry
monomer
-
1 * 27000, recombinant AroE, SDS-PAGE, 1 * 27076, recombinant AroE, mass spectrometry
-
additional information
SDH enzymes exist in opened and closed conformational states. In the ternary structure of Aquifex aeolicus SDH (PDB ID 2HK9), three loops in the shikimate binding domain are shifted about 5 A toward the NADP++ binding site compared to their position in an unliganded structure of the same enzyme (PDB ID 2HK8). The closed form of the structure thus brings the bound shikimate and NADP+ molecules into close proximity, facilitating a hydride transfer between the shikimate C5-hydroxyl and C4 of the NADP+ nicotinamide ring
additional information
the SDH domain is connected via its N-terminus to the DHQ module
additional information
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structure analysis, dynamic light scattering measurements
additional information
three-dimensional structure analysis of AroE
additional information
the active subpocket 1 is formed by residues Val8, Ser16, Ser18, Asn63, Val64, Thr65, Lys69, Asn90, Asp105, and Gln237, subpocket 2 by residues Asp105, Ser129, Ala179, Thr180, Ser181, Leu184, Leu208, Tyr210, Gly230, Met233, and Leu234, and subpocket 3 by residues Gly125, Ala126, Gly127, Asn148, Arg149, Ser150, Thr180, Ser181, Ala182, and Pro189
additional information
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the active subpocket 1 is formed by residues Val8, Ser16, Ser18, Asn63, Val64, Thr65, Lys69, Asn90, Asp105, and Gln237, subpocket 2 by residues Asp105, Ser129, Ala179, Thr180, Ser181, Leu184, Leu208, Tyr210, Gly230, Met233, and Leu234, and subpocket 3 by residues Gly125, Ala126, Gly127, Asn148, Arg149, Ser150, Thr180, Ser181, Ala182, and Pro189
additional information
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the structure reveals an enzyme with a deep cleft, which contains the active site, formed at the junction of two domains. The C-terminal domain is easily recognizable as a Rossmann fold dinucleotide binding domain, responsible for binding the NADP cofactor. The N-terminal substrate binding and dimerization domain, an alpha-beta-alpha sandwich, represents a unique topological fold, structure modeling
additional information
the enzyme shows an alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively, a phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site, the structure reveals a topologically unique domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization, homology modeling, overview
additional information
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the enzyme shows an alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively, a phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site, the structure reveals a topologically unique domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization, homology modeling, overview
additional information
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secondary structure analysis of ARoE, percentages for alpha-helix, beta-sheet, beta-turn, and random coil are 29.2%, 9.3%, 32.7%, and 28.8%, respectively, contains the highly conserved motif G-X-(N/S)-V-(T/S)-X-PX-K
additional information
three-dimensional structure analysis of wild-type and mutant enzymes with bound substrates, overview
additional information
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three-dimensional structure analysis of wild-type and mutant enzymes with bound substrates, overview
additional information
the overall structure of SDH comprises two alpha/beta domains linked centrally by two alpha-helices. A deep groove between these two domains contains the active site for the binding of substrate and cofactor
additional information
-
the overall structure of SDH comprises two alpha/beta domains linked centrally by two alpha-helices. A deep groove between these two domains contains the active site for the binding of substrate and cofactor
additional information
-
three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
additional information
-
the DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
additional information
-
three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
-
additional information
-
the DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
-
additional information
-
three-dimensional structure determination by homology modelling and validation
additional information
-
three-dimensional structure determination by homology modelling and validation
-
additional information
-
structural modeling of TgSDH suggests that the protein's three large amino acid insertions form surface-exposed loops with alpha-helical character, structure modelling and structure comparisons, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-enzyme and in complex with both shikimate and NADP+, which assumes the closed conformation
analysis of three-dimensional crystal structure of enzyme DHQD-SDH with shikimate bound in the SDH active site, PDB ID 2GPT. Crystallization of T381G mutant bound with quinate
crystal structure analysis, PDB IDs 2GPT, 2O7Q, and 2O7S, for the binary and ternary complexes of enzyme and substrates
in complex with shikimate, and in ternary complex with shikimate and NADP+
-
purified native and selenomethionine-labeled DELTA88DHQ-SDH complexed with shikimate, hanging drop vapour diffusion method, 10 mg/ml protein in 1 mM shikimate mixed with equal volume of reservoir solution containing 0.4 M potassium sodium tartrate tetrahydrate, 0.1 M tri-sodium dihydrate, pH 5.6, and 2.8 M ammonium sulfate, X-ray diffraction structure determination and analysi at 1.95-2.2 A resolution
-
crystallized at 23°C using ammonium sulfate as a precipitant. Crystals grown in the presence of NADP+ diffract to 2.8 A resolution and belong to the trigonal space group P3(2)21 (or P3(2)21), with unit-cell parameters a = 111.3, b = 111.3, c = 76.2 A
in complex with NADP+, to 2.8 A resolution. Crystal belong to space group P3221
purified recombinant enzyme, sitting drop vapour diffusion method, 3.75 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 0.5 M NaCl, 1 mM NaN3, and 20% v/v glycerol, the reservoir solution contains 0.1 M sodium acetate, pH 4.6, 0.2 M NaCl, and 20% v/v precipitant 2,4-methylenepentanediol, 0.002 ml of protein, reservoir and 0.002 mM NADH solutions are mixed at 20°C, about 5 months, formation of rod- and needle-shaped crystals, X-ray diffraction structure determination and analysis at 1.64 A resolution
-
purified recombinant enzyme, 20 mg/ml in 10 mM Tris-HCl, pH 7.6, 0.4 mM DTT, and 2.5 mM NADPH, 20°C, sitting-drop vapour-diffusion method, reservoir solution contains 1.65 M ammonium sulfate, 100 mM cacodylate buffer, pH 5.8, 1.5 ml of protein solution is mixed with an equal volume of reservoir solution, 10-12 days, cryoprotection with 20% v/v glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
catalytic domain with open twisted alpha/beta motif plus NADPH binding domain with typical Rossman fold
purified recombinant wild-type and selenomethionine-labeled paralogue HI0607, hanging drop vapour diffusion method, 0.001 ml protein solution containing 20 mg/ml protein mixed with equal volume of reservoir solution containing 0.1 M sodium acetate, pH 4.6, 2.0 M NaCl, and 10% v/v PEG 400, X-ray diffraction structure determination and analysis at 1.75 A resolution
-
wild-type and selenomethionine-labeled enzyme, free and in complex with NADPH, sitting drop vapour diffusion method, 10 mg/m protein, with or without 5 mM NADPH, mixture in a ratio of 1:1 with crystallization solution containing 1.0 M sodium citrate, and 0.1 M 2-(cyclohexylamino)ethanesulfonic acid (CHES), pH 8.8, for the free enzyme, and 12% PEG 8000, 0.15 M calcium acetate, pH 7.8, and 0.1 M imidazole for the selenomethionine-labeled enzyme, 4°C, X-ray diffraction structure determination and analysis at 2.4 A and 1.95 A, respectively, structure modeling
determination of diverse crystal structures with apoenzyme, or enzyme in binary or ternary complexes
-
in complex with NADP+, compact alpha/beta sandwich with two domains for binding substrate and cofactor, resp.
purified recombinant AroE bound to cofactor NADP+, hanging drop vapour diffusion method at 25°C, 10 mg/ml protein in 20 mM HEPES, pH 7.1, and 0.1 M KCl, is mixed with reservoir solution containing 20 mM HEPES, pH 7.1, 20% PEG 3350, and 0.2 M ammonium fluoride, cryoprotection with 15% glycerol, X-ray diffraction structure determination and analysis at 2.35 A resolution
homology modeling and circular dichroism study. NADP+ binding results in small conformational changes
-
crystal structure determination of apoenzyme, PDB ID 3DON, and shikimate-bound binary enzyme complex, PDB ID 3DOO
at 4°C, using the hanging-drop vapor-diffusion method. SDH both in its ligand-free form and in complex with shikimate. Overall structure of apo-SDH is basically identical to that of the shikimate-SDH complex, both structures contain one molecule per asymmetric unit. Overall folding of SDH comprises the N-terminal alpha/beta domain for substrate binding and the C-terminal Rossmann fold for NADP binding. The active site is within a large groove between the two domains. Residue Tyr211 does not interact with shikimate in the binary SDH-shikimate complex structure. The main function of Tyr211 may be to stabilize the catalytic intermediate during catalysis. The NADP-binding domain of SDH is less conserved. The long helix specifically recognizing the adenine ribose phosphate is substituted with a short 310 helix in the NADP-binding domain. The interdomain angle of SDH is the widest among all known SDH structures, indicating an inactive open state of the SDH structure. Thus, a closing process may occur upon NADP+ binding to bring the cofactor close to the substrate for catalysis
determination of the crystal structure at 1.45 A by molecular replacement. The protein shows a monomeric architecture. The overall structure comprises the N-terminal alpha/beta sandwich domain for substrate binding and the C-terminal domain for NADP binding.the enzyme is in a tightly closed conf ormation, which should be open for catalysis. Four ammonium sulfate ions were identified in the structure. They are located in the active site and appear to mimic the role of the substrate in terms of the enzyme activity and stability
ligand-free form, binary complexes with NADP+ or substrate shikimate, and ternary complex with both NADP+ and shikimate. Structures of the closed subunits with and without NADP(H) show no significant difference. Residues K64 and D100 are involved in hydride transfer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D423A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, inactive mutant
D423N
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
K385A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
K385N
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
K385N/D423N
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
S336A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
S338A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
S338G
site-directed mutagenesis, the mutant is not active with quinate like the wild-type
S338G/T381G
site-directed mutagenesis, the double mutant does not show improved enzymatic activity with quinate compared with the T381G mutant
T381A
T381G
site-directed mutagenesis, mutant shows increased activity with quinate compared to wild-type, it catalyzes the oxidation of quinate with a turnover rate of 8.8/s and a KM of 3.33 mM
T381S
T407A
-
site-directed mutagenesis, 6.5fold decrease in kcat value, increase in Km-value
Y550A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Y550F
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
G338S/G381T/D483N/L484R/D485T
site-directed mutagenesis, mutant MTCsDQD/SDHb has a similar reduction activity of 3-DHS and had six times higher oxidation activity of SA than wild-type isozyme CsDQD/SDHb, suggesting that the mutation of residues Ser338 and NRT to Gly and DI/LD in the SDH unit is the reason for the low activity of CsDQD/SDHb, respectively
A243G
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
D195E
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
N149D
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
N149D/V152F
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A/L135A
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A/L135A/N149D/V152F
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A/N149D/V152F
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
D103X
-
site-directed mutagenesis of paralogue HI0607, inactive mutant
K69A
-
site-directed mutagenesis, the mutant shows significantly reduced the catalytic efficiency compared to wild-type enzyme
A213L
site-directed mutagenesis, analysis of substrate and cofactor binding compared to wild-type enzyme
D105A
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
D105N
K69A
K69H
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
K69I
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
K69Q
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
S275G
-
site-directed mutagenesis, the mutant shows only slightly reduced maximum activity with shikimate compared with wild-type PoptrSDH1
S275G/T318G
-
site-directed mutagenesis, the double mutant is well expressed in Escherichia coli and shows bona fide QDH activity besides its original SDH activity, which is severely reduced. Although the Ser275Gly/Thr318Gly double mutant is clearly sufficient to confer gain of activity with quinate, its activity is lower than the QDH activities of PintaQDH and PoptrQDH2 activity
T318G
-
site-directed mutagenesis, the Thr318Gly mutant yields only a very small amount of enzyme when recombinantly expressed in Escherichia coli
Y211F
results in a remarkable reduction in enzyme activity, leads to a significant decrease in kcat (345fold) and a minor increase in the Km (3fold) for shikimate. Tyr211 may play a major role in the catalytic process and a minor role in the initial substrate binding
additional information
T381A
-
site-directed mutagenesis, more than twentyfold decrease in kcat value
T381A
site-directed mutagenesis, the mutant accepts quinate as a substrate but is much less efficient than the T381G variant
T381S
-
site-directed mutagenesis, fourfold decrease in kcat value, slight decrease in Km value
T381S
site-directed mutagenesis, the mutant accepts quinate as a substrate but is much less efficient than the T381G variant
D105N
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
D105N
site-directed mutagenesis, analysis of substrate and cofactor binding compared to wild-type enzyme
K69A
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid. Best recombinant protein expression protocol of the K69A mutant in insoluble form is using Escherichia coli C41(DE3) strain, grown at 37°C for 24 h after induction with 1 mM IPTG, and cell disruption by sonication
K69A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, overview
K69A
site-directed mutagenesis, analysis of substrate and cofactor binding compared to wild-type enzyme
additional information
-
construction of deletion variant DELTA88DHQ-SDH, thermal denaturation analysis, overview
additional information
absence of the T381 side chain creates sufficient space in the active site to accommodate the quinate C1-hydroxyl. The K385 and D423 catalytic dyad which interacts with C4-OH and participates in proton transfer during the reduction/oxidation of NADP+/NADPH is retained in the T381G mutant
additional information
referring to the model of Arabidopsis thaliana protein crystal structure, the amino acid residue sites of Gly338, Gly381, Asp483, Leu484, and Asp485 in CsDQD/SDHb are mutated to Ser338, Thr381, Asn483, Arg484, and Thr485, respectively, the mutant protein is named MTCsDQD/SDHb
additional information
-
referring to the model of Arabidopsis thaliana protein crystal structure, the amino acid residue sites of Gly338, Gly381, Asp483, Leu484, and Asp485 in CsDQD/SDHb are mutated to Ser338, Thr381, Asn483, Arg484, and Thr485, respectively, the mutant protein is named MTCsDQD/SDHb
additional information
steady state cytosolic free and whole cell NADPH/NADP ratio in different Saccharomycs cerevisiae strains, with or without recombinant expression of shikimate dehydrogenase from Escherichia coli, thermodynamics and kinetics, overview
additional information
invertion of the cofactor specificity from NADP+ to NAD+ on the Escherichia coli wild-type enzyme, effect of consensus mutations, overview. Mutant structure modeling
additional information
-
invertion of the cofactor specificity from NADP+ to NAD+ on the Escherichia coli wild-type enzyme, effect of consensus mutations, overview. Mutant structure modeling
additional information
ydiB-encoded enzyme knockout in Escherichia coli strain PB12
additional information
-
ydiB-encoded enzyme knockout in Escherichia coli strain PB12
-
additional information
-
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
additional information
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
additional information
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
additional information
-
suppression of shikimate dehydrogenase activity by RNAi. Transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin. Dehydroquinate, the substrate of the enzyme, accumulates, and due to a second, cytosolic enzyme, the product, shikimate accumulates
additional information
suppression of shikimate dehydrogenase activity by RNAi. Transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin. Dehydroquinate, the substrate of the enzyme, accumulates, and due to a second, cytosolic enzyme, the product, shikimate accumulates
additional information
suppression of shikimate dehydrogenase activity by RNAi. Transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin. Dehydroquinate, the substrate of the enzyme, accumulates, and due to a second, cytosolic enzyme, the product, shikimate accumulates
additional information
-
cytosolic isoform cannot complement loss of the plastidial isoform
additional information
cytosolic isoform cannot complement loss of the plastidial isoform
additional information
cytosolic isoform cannot complement loss of the plastidial isoform
additional information
the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Staphyococcus epidermidis SDH causes a substantial reduction in turnover rate
additional information
-
the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Staphyococcus epidermidis SDH causes a substantial reduction in turnover rate
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
55
purified recombinant AroE, 20% remaining activity after 1 h
60
87
60
-
complete inactivation after 10 min, at 50-55°C biphasic, inactivation can be minimized with bound substrate to about 60%
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM Tris-HCl buffer, pH 7.5, 500 mM NaCl, 5% glycerol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by nickel-nitrilotriacetic acid affinity chromatography
Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4 °C in 10 mM TrisHCl, 500 mM NaCl, and 5% glycerol.
Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4°C in 10 mM Tris-HCl, 500 mM NaCl, and 5% glycerol.
Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4°C in 10 mM TrisHCl, 500 mM NaCl, and 5% glycerol.
homogeneous recombinant mutant K69A and wild-type proteins are obtained by a three-step purification protocol, by gel filtration, 11.8fold
-
one-step purification by nickel-affinity chromatography
recombinant CsDQD/SDH isozymes from Escherichia coli strain NovaBlue (DE3) by maltose affinity chromatography and ultrafiltration
recombinant enzyme expressed in Escherichia coli, formation of insoluble aggregates, solubilization by repeated freezing and thawing
-
recombinant enzyme from aroE auxotrophic mutant strain AB2834 by ammonium sulfate fractionation, anion exchange chromatography, ultrafiltration, and gel filtration
-
recombinant GST-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by glutathione affinity chromatography and tag cleavage through thrombin
recombinant GST-tagged SeMet-labeled enzyme from Escherichia coli strain BL21 by glutathione affinity and ion exchange chromatography, proteolytic removal of the GST-tag
recombinant His-tagged ARoE from Escherichia coli strain BL21(DE3) by nickel affinity chromatograohy
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and dialysis
recombinant His6-tagged DQD/SDH isozyme 5 from Escherichia coli strain M15 by nickel affinity chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus by nickel affinity chromatography and dialysis
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography
-
recombinant soluble enzyme 8.5fold from Escherichia coli strain BL21(DE3) by ion exchange and hydrophobic interaction chromatography, gel filtration, and again ion exchange chromatography, to homogeneity
recombinant His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus by nickel affinity chromatography and dialysis
recombinant His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus by nickel affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of Hs6-tagged isozyme 1 in Escherichia coli, transfection of Nicotina plants
expression in Escherichia coli
expression in Escherichia coli as recombinant N-terminal GST-tagged protein
expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of wild-type and selenomethionine-labeled enzyme in Escherichia coli strain DL41
five putative SDH-encoding genes amplified and cloned into either a modified pET28a vector or the p15TVLIC vector, a ligation-independent vector due to incompatible cloning sites between the insert and pET28.3. Expressed in either the Escherichia coli strain BL21 gold (p15TV-LIC constructs) or the Escherichia coli BL21CodonPlus (pET28.3constructs)
gene aroE from Escherichia coli sstrain DH5alpha, recombinant overexpression in Saccharomyces cerevisiae strain CEN.PK 113-5D yielding strain CEN.PK-aroE
gene aroE, DNA and amino acid sequence determination, functional expression as soluble enzyme in Escherichia coli strain BL21(DE3)
gene aroE, expression of GST-tagged SeMet-labeled enzyme in Escherichia coli strain BL21
gene aroE, expression of His-tagged AroE in Escherichia coli strain BL21(DE3)
-
gene aroE, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene aroE, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
gene aroE, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 CodonPlus
gene aroE, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
-
gene EcDQD/SDH1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL, quantitative real-time RT-PCR enzyme expression analysis
gene EcDQD/SDH2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL, quantitative real-time RT-PCR enzyme expression analysis
gene EcDQD/SDH3, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL, quantitative real-time RT-PCR enzyme expression analysis
gene SDH, phylogenetic analysis
gene ydiB, the ydiB gene is cloned into plasmid pTOPO aroB aroE, resulting in the pTOPO ydiB aroB aroE derivative, enzyme overexpression in Escherichia coli strain PB12, quantitative RT-PCR analysis, coexpression of plasmid pTOPO aroB aroE and pJLB aroG fbr tktA and the cultivation of this derivative in Escherichia coli strain PB12.SA2 resulting in very high level expression of gene ydiB during exponential and stationary growth stages
genes encoding PgSDH1, PgSDH3-1,2, PgSDH3a-1,2, and PgSDH4, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genes PgSDH3 and PgSDH3a occur in tandem
isozyme VvSDH1, sequence comparison and phylogenetic analysis and tree, recombinant expression
isozyme VvSDH2, sequence comparison and phylogenetic analysis and tree, recombinant expression
isozyme VvSDH3, sequence comparison and phylogenetic analysis and tree, recombinant expression
isozyme VvSDH4, sequence comparison and phylogenetic analysis and tree, recombinant expression
multiple DQD/SDH protein sequences are obtained from Phytozome 12.0 and NCBI, phylogenetic analysis and tree, recombinant expression of CsDQD/SDH isozymes in Escherichia coli strain NovaBlue (DE3)
overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
phylogenetic analysis of the three paralogues YdiB, AroE, and HI0607, DNA and amino acid sequence determination and analysis of paralogue HI0607, expression of wild-type paralogue HI0607 in Escherichia coli strain BL21(DE3) and of selenomethionine-labeled enzyme in strain B834(DE3)
-
plasmid pET23a(+)::aroE (either wild-type or mutants) transformed into Escherichia coli C41(DE3)
-
recombinant His6-tagged DQD/SDH isozyme 1 overexpression in Escherichia coli strain M15
-
recombinant His6-tagged DQD/SDH isozyme 5 overexpression in Escherichia coli strain M15
-
SDH-encoding gene is amplified by polymerase chain reaction from Pseudomonas putida KT2440 genomic DNA using primers with incorporated restriction sites. Resulting product is cloned into a vector and expressed in the Escherichia coli strain BL21 with appropriate antibiotics.
SDH-encoding gene is amplified by polymerase chain reaction from Pseudomonas putida KT2440 genomic DNA using primers with incorporated restriction sites. Resulting product is cloned into vector and expressed in the Escherichia coli strain BL21 with appropriate antibiotics.
wild-type and mutant cloned into vector pET22b and transformed into Escherichia coli strain BL21(DE3). Selenomethionine-substituted SDH generated in the methionine auxotrophic Escherichia coli strain B834(DE3)
gene aroE, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 CodonPlus
gene aroE, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 CodonPlus
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
immediately following application of hypoosmotic stress, the activity of the enzyme in leaves decreases compared to plants grown in soil. After 3 days, a defense response appears in the form of substantially (2.3fold) increased specific activities in hypoosmotically stressed leaves
isoform qsuD mRNA expression in shikimate-grown cells is upregulated relative to that in the glucose-grown cells
the expression of PgSDH1, which presumably contributes to shikimate biosynthesis, was relatively constant at different sucrose concentrations. The transcript levels of PgSDH3s and PgSDH4 increased with the accumulation of gallic acid and HTs under osmotic stress, which apparently accumulates to protect the cells from the stress
isoform qsuD mRNA expression in shikimate-grown cells is upregulated relative to that in the glucose-grown cells
A4QEK4, A4QB65
isoform qsuD mRNA expression in shikimate-grown cells is upregulated relative to that in the glucose-grown cells
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme is stable up to 50°C presenting a cooperative unfolding profile. Unfolding at 63°C is irreversible
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
usage of Escherichia coli shikimate dehydrogenase as sensor reaction for determination of the cytosolic NADPH/NADP ratio in Saccharomyces cerevisiae, quantitative measurements of physiological variables in the cytosolic compartment by GC-MS/MS, cytosolic NADPH/NADP ratio in batch experiments, overview. The steady state sensor reaction based cytosolic free NADPH/NADP ratio is 15.6
diagnostics
-
shikimate dehydrogenase alleles can act as potential markers for flowering phenology in Pinus sylvestris. The ShDH A locus might be considered as isoenzymatic marker that differentiates these flowering groups of Scots pine clones. At several isozyme and DNA loci, the presence of private alleles in each group of pines is observed, but these alleles cannot serve as markers of Scots pine flowering time because of their low frequencies
drug development
food industry
the biosynthesis of anthocyanins (ATs) and hydrolysable tannins (HTs) competes for the same substrate, 3-DHS, and SDH activity is regulated not only by the NADPH/NADP+ ratio, but also by the expression of the pomegranate shikimate dehydrogenases, PgSDHs. Since the outer peel affects the customer's decision regarding fruit consumption, such knowledge can be utilized for the development of genetic markers for breeding pomegranates having higher levels of both ATs and HTs
agriculture
the enzyme is a target for the development of herbicides and antimicrobial agents
agriculture
-
the enzyme is a target for the development of herbicides and antimicrobial agents
-
drug development
the enzyme can be a target for rational design of specific inhibitors, aiming at the development of antitubercular drugs
drug development
-
shikimate dehydrogenase is an essential protein for the biosynthesis of the chorismate end product and is a highly promising therapeutic target, especially for the discovery and development of new-generation anti-tuberculosis agents
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
drug development
-
the essential enzyme is a potential target for antimicrobials
drug development
-
the essential enzyme is a potential target for herbicides and antimicrobials
drug development
-
the essential enzyme is a potential target for herbicides and antimicrobials
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
drug development
-
the enzyme is a target for antibacterial drug development
drug development
-
the essential enzyme is a potential target for herbicides and antimicrobials
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
drug development
the enzyme is a promising target for antituberculosis agent development
drug development
-
the enzyme is a target for drug development required for Acinetobacter baumannii, a member of ESKAPE pathogens, that has emerged as an extreme drug-resistant bacterium towards most of the current generation. Acinetobacter baumannii demonstrates resistance to nearly all major classes of antibiotics, including broad-spectrum penicillins, carbapenems, cephalosporins, fluoroquinolones, aminoglycosides, tetracyclines, chloramphenicol, and colistin, especially polymixin, creating a public health threat worldwide
drug development
-
shikimate dehydrogenase is an essential protein for the biosynthesis of the chorismate end product and is a highly promising therapeutic target, especially for the discovery and development of new-generation anti-tuberculosis agents
-
drug development
-
the essential enzyme is a potential target for herbicides and antimicrobials
-
drug development
-
the essential enzyme is a potential target for herbicides and antimicrobials
-
drug development
-
the essential enzyme is a potential target for herbicides and antimicrobials
-
drug development
-
the essential enzyme is a potential target for herbicides and antimicrobials
-
drug development
-
the enzyme is a target for antibacterial drug development
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jacobson, J.W.; Hart, B.A.; Doy, C.H.; Giles, N.H.
Purification and stability of the multienzyme complex encoded in the arom gene cluster of Neurospora crassa
Biochim. Biophys. Acta
289
1-12
1972
Neurospora crassa
brenda
Polley, L.D.
Purification and characterization of 3-dehydroquinate hydrolase and shikmate oxidoreductase. Evidence for a bifunctional enzyme
Biochim. Biophys. Acta
526
259-266
1978
Physcomitrium patens
brenda
Chaudhuri, S.; Coggins, J.R.
The purification of shikimate dehydrogenase from Escherichia coli
Biochem. J.
226
217-223
1985
Escherichia coli
brenda
Lourenco, E.J.; Neves, V.A.
Partial purification and some properties of shikimate dehydrogenase from tomatoes
Phytochemistry
23
497-499
1984
Solanum lycopersicum
-
brenda
Koshiba, T.
Purification of two forms of the associated 3-dehydroquinate hydro-lyase and shikimate:NADP+ oxidoreductase in Phaseolus mungo seedlings
Biochim. Biophys. Acta
522
10-18
1978
Vigna mungo
brenda
Sanderson, G.W.
5-Dehydroshikimate reductase in the tea plant (Camellia sinensis L.). Properties and distribution
Biochem. J.
98
248-252
1966
Camellia sinensis
brenda
Higuchi, T.; Shimada, M.
Changes in activity of shikimate:NADP oxidoreductase in relation to lignification of bamboo
Plant Cell Physiol.
8
61-69
1967
Bambusa sp.
-
brenda
Balinsky, D.; Davies, D.D.
Aromatic biosynthesis in higher plants I. Preparation and properties of dehydroshikimic reductase
Biochem. J.
80
292-296
1961
Lathyrus oleraceus
brenda
Lemos Silva, G.M.; Lourenco, E.J.; Neves, V.A.
Inhibition of shikimate dehydrogenase from heart-of-palm (Euterpe oleracea Mart.)
J. Food Biochem.
9
105-116
1985
Euterpe oleracea
-
brenda
Yaniv, H.; Gilvarg, C.
Aromatic biosynthesis. XIV. 5-dehydroshikimic reductase
J. Biol. Chem.
213
787-795
1955
Escherichia coli
brenda
Maclean, J.; Campbell, S.A.; Pollock, K.; Chackrewarthy, S.; Coggins, J.R.; Lapthorn, A.J.
Crystallization and preliminary X-ray analysis of shikimate dehydrogenase from Escherichia coli
Acta Crystallogr. Sect. D
56
512-515
2000
Escherichia coli
brenda
Lourenco, E.J.; Silva, G.M.L.; Neves, V.A.
Purification and properties of shikimate dehydrogenase from cucumber (Cucumis sativa L.)
J. Agric. Food Chem.
39
458-462
1991
Cucumis sativus
-
brenda
Diaz, J.; Merino, F.
Shikimate dehydrogenase from pepper (Capsicum annuum) seedlings. Purification and properties
Physiol. Plant.
100
147-152
1997
Capsicum annuum
-
brenda
Lim, S.; Schroder, I.; Monbouquette, H.G.
A thermostable shikimate 5-dehydrogenase from the archaeon Archaeoglobus fulgidus
FEMS Microbiol. Lett.
238
101-106
2004
Archaeoglobus fulgidus
brenda
Ye, S.; Von Delft, F.; Brooun, A.; Knuth, M.W.; Swanson, R.V.; McRee, D.E.
The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode
J. Bacteriol.
185
4144-4151
2003
Haemophilus influenzae, Haemophilus influenzae (P43876)
brenda
Magalhaes, M.L.; Pereira, C.P.; Basso, L.A.; Santos, D.S.
Cloning and expression of functional shikimate dehydrogenase (EC 1.1.1.25) from Mycobacterium tuberculosis H37Rv
Protein Expr. Purif.
26
59-64
2002
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Padyana, A.K.; Burley, S.K.
Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution
Structure
11
1005-1013
2003
Methanocaldococcus jannaschii (Q58484), Methanocaldococcus jannaschii
brenda
Schoepe, J.; Niefind, K.; Chatterjee, S.; Schomburg, D.
Cloning, expression, purification and preliminary crystallographic characterization of a shikimate dehydrogenase from Corynebacterium glutamicum
Acta Crystallogr. Sect. F
F62
635-637
2006
Corynebacterium glutamicum
brenda
Singh, S.A.; Christendat, D.
Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway
Biochemistry
45
10406
2006
Arabidopsis thaliana
brenda
Adachi, O.; Ano, Y.; Toyama, H.; Matsushita, K.
Purification and properties of NADP-dependent shikimate dehydrogenase from Gluconobacter oxydans IFO 3244 and its application to enzymatic shikimate production
Biosci. Biotechnol. Biochem.
70
2786-2789
2006
Gluconobacter oxydans, Gluconobacter oxydans IFO 3244
brenda
Han, C.; Wang, L.; Yu, K.; Chen, L.; Hu, L.; Chen, K.; Jiang, H.; Shen, X.
Biochemical characterization and inhibitor discovery of shikimate dehydrogenase from Helicobacter pylori
FEBS J.
273
4682-4692
2006
Helicobacter pylori (Q56S04), Helicobacter pylori, Helicobacter pylori SS1 (Q56S04)
brenda
Zhang, X.; Zhang, S.; Hao, F.; Lai, X.; Yu, H.; Huang, Y.; Wang, H.
Expression, purification and properties of shikimate dehydrogenase from Mycobacterium tuberculosis
J. Biochem. Mol. Biol.
38
624-631
2005
Mycobacterium tuberculosis
brenda
Singh, S.; Korolev, S.; Koroleva, O.; Zarembinski, T.; Collart, F.; Joachimiak, A.; Christendat, D.
Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae
J. Biol. Chem.
280
17101-17108
2005
Haemophilus influenzae
brenda
Fonseca, I.O.; Magalhaes, M.L.; Oliveira, J.S.; Silva, R.G.; Mendes, M.A.; Palma, M.S.; Santos, D.S.; Basso, L.A.
Functional shikimate dehydrogenase from Mycobacterium tuberculosis H37Rv: purification and characterization
Protein Expr. Purif.
46
429-437
2006
Mycobacterium tuberculosis (A5U5Q2), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (A5U5Q2), Mycobacterium tuberculosis H37Rv
brenda
Vogan, E.
Shikimate dehydrogenase structure reveals novel fold
Structure
11
902-903
2003
Methanocaldococcus jannaschii
brenda
Ding, L.; Hofius, D.; Hajirezaei, M.R.; Fernie, A.R.; Boernke, F.; Sonnewald, U.
Functional analysis of the essential bifunctional tobacco enzyme 3-dehydroquinate dehydratase/shikimate dehydrogenase in transgenic tobacco plants
J. Exp. Bot.
58
2053-2067
2007
Nicotiana tabacum, Nicotiana tabacum (Q6PUG0), Nicotiana tabacum (Q6PUF9)
brenda
Schoepe, J.; Niefind, K.; Schomburg, D.
1.6 A structure of an NAD(+)-dependent quinate dehydrogenase from Corynebacterium glutamicum
Acta Crystallogr. Sect. D
64
803-809
2008
Corynebacterium glutamicum (Q9X5C9)
brenda
Fonseca, I.O.; Silva, R.G.; Fernandes, C.L.; de Souza, O.N.; Basso, L.A.; Santos, D.S.
Kinetic and chemical mechanisms of shikimate dehydrogenase from Mycobacterium tuberculosis
Arch. Biochem. Biophys.
457
123-133
2007
Mycobacterium tuberculosis (A5U5Q2), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (A5U5Q2)
brenda
Gan, J.; Wu, Y.; Prabakaran, P.; Gu, Y.; Li, Y.; Andrykovitch, M.; Liu, H.; Gong, Y.; Yan, H.; Ji, X.
Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism
Biochemistry
46
9513-9522
2007
Aquifex aeolicus (O67049), Aquifex aeolicus
brenda
Singh, S.A.; Christendat, D.
The DHQ-dehydroshikimate-SDH-shikimate-NADP(H) complex: insights into metabolite transfer in the shikimate pathway
Cryst. Growth Des.
7
2153-2160
2007
Arabidopsis thaliana
-
brenda
Bagautdinov, B.; Kunishima, N.
Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism
J. Mol. Biol.
373
424-438
2007
Thermus thermophilus (Q5SJF8), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SJF8)
brenda
Arcuri, H.A.; Borges, J.C.; Fonseca, I.O.; Pereira, J.H.; Neto, J.R.; Basso, L.A.; Santos, D.S.; de Azevedo, W.F.
Structural studies of shikimate 5-dehydrogenase from Mycobacterium tuberculosis
Proteins
72
720-730
2008
Mycobacterium tuberculosis
brenda
Singh, S.; Stavrinides, J.; Christendat, D.; Guttman, D.S.
A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass
Mol. Biol. Evol.
25
2221-2232
2008
Pseudomonas putida (Q88RQ5), Pseudomonas putida (Q88IJ7), Pseudomonas putida (Q88K85), Pseudomonas putida (Q88JP1), Pseudomonas putida (Q88GF6), Pseudomonas putida KT 2240 (Q88RQ5), Pseudomonas putida KT 2240 (Q88IJ7), Pseudomonas putida KT 2240 (Q88K85), Pseudomonas putida KT 2240 (Q88JP1), Pseudomonas putida KT 2240 (Q88GF6), Pseudomonas putida KT2440 (Q88RQ5), Pseudomonas putida KT2440 (Q88IJ7)
brenda
Han, C.; Hu, T.; Wu, D.; Qu, S.; Zhou, J.; Ding, J.; Shen, X.; Qu, D.; Jiang, H.
X-ray crystallographic and enzymatic analyses of shikimate dehydrogenase from Staphylococcus epidermidis
FEBS J.
276
1125-1139
2009
Staphylococcus epidermidis RP62A (Q5HNV1)
brenda
Rodrigues, V.d.a..S.; Basso, L.A.; Santos, D.S.
Homogeneous recombinant Mycobacterium tuberculosis shikimate dehydrogenase production: an essential step towards target-based drug design
Int. J. Biol. Macromol.
45
200-205
2009
Mycobacterium tuberculosis
brenda
Barcellos, G.B.; Caceres, R.A.; de Azevedo, W.F.
Structural studies of shikimate dehydrogenase from Bacillus anthracis complexed with cofactor NADP
J. Mol. Model.
15
147-155
2009
Bacillus anthracis
brenda
Cao, S.; Hu, Z.; Zheng, Y.; Lu, B.
Effect of BTH on anthocyanin content and activities of related enzymes in Strawberry after harvest
J. Agric. Food Chem.
58
5801-5805
2010
Fragaria x ananassa
brenda
Rodrigues, V.S.; Breda, A.; Santos, D.S.; Basso, L.A.
The conserved Lysine69 residue plays a catalytic role in Mycobacterium tuberculosis shikimate dehydrogenase
BMC Res. Notes
2
227
2009
Mycobacterium tuberculosis (P95001), Mycobacterium tuberculosis, no activity in Homo sapiens
brenda
Lee, H.H.
Overexpression, crystallization and preliminary X-ray crystallographic analysis of shikimate dehydrogenase from Archaeoglobus fulgidus
Acta Crystallogr. Sect. F
67
1556-1558
2011
Archaeoglobus fulgidus (O27957), Archaeoglobus fulgidus, Archaeoglobus fulgidus ATCC 49558 (O27957)
brenda
Lee, H.H.
Overexpression, crystallization, and preliminary X-ray crystallographic analysis of shikimate dehydrogenase from Thermotoga maritima
Acta Crystallogr. Sect. F
67
824-826
2011
Thermotoga maritima (Q9WYI1), Thermotoga maritima, Thermotoga maritima ATCC 43589 (Q9WYI1)
brenda
Kubota, T.; Tanaka, Y.; Hiraga, K.; Inui, M.; Yukawa, H.
Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
97
8139-8149
2013
Corynebacterium glutamicum (A4QEK4), Corynebacterium glutamicum (A4QB65), Corynebacterium glutamicum, Corynebacterium glutamicum JCM 18229 (A4QEK4), Corynebacterium glutamicum JCM 18229 (A4QB65)
brenda
Lee, H.H.
High-resolution structure of shikimate dehydrogenase from Thermotoga maritima reveals a tightly closed conformation
Mol. Cells
33
229-233
2012
Thermotoga maritima (Q9WYI1), Thermotoga maritima, Thermotoga maritima ATCC 43589 (Q9WYI1)
brenda
Peek, J.; Christendat, D.
The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework
Arch. Biochem. Biophys.
566
85-99
2015
Aquifex aeolicus (O67049), Arabidopsis thaliana (Q9SQT8), Archaeoglobus fulgidus (O27957), Archaeoglobus fulgidus ATCC 49558 (O27957), Aspergillus nidulans (P07547), Aspergillus nidulans FGSC A4 (P07547), Corynebacterium glutamicum (A4QB65), Escherichia coli, Helicobacter pylori, Mycobacterium tuberculosis, Populus trichocarpa, Pseudomonas putida (Q88IJ7), Pseudomonas putida KT 2240 (Q88IJ7), Staphylococcus aureus, Staphylococcus epidermidis (Q5HNV1), Staphylococcus epidermidis ATCC 35984 (Q5HNV1), Toxoplasma gondii (Q6W3D0)
brenda
Prus-Glowacki, W.; Sukovata, L.; Lewandowska-Wosik, A.; Nowak-Bzowy, R.
Shikimate dehydrogenase (E.C. 1.1.1.25 ShDH) alleles as potential markers for flowering phenology in Pinus sylvestris
Dendrobiology
73
153-162
2015
Pinus sylvestris
-
brenda
Guo, J.; Carrington, Y.; Alber, A.; Ehlting, J.
Molecular characterization of quinate and shikimate metabolism in Populus trichocarpa
J. Biol. Chem.
289
23846-23858
2014
Populus trichocarpa, Populus trichocarpa Nisqually-1
brenda
Peek, J.; Shi, T.; Christendat, D.
Identification of novel polyphenolic inhibitors of shikimate dehydrogenase (AroE)
J. Biomol. Screen.
19
1090-1098
2014
Arabidopsis thaliana (Q9SQT8), Arabidopsis thaliana, Pseudomonas putida (Q88RQ5), Pseudomonas putida, Pseudomonas putida KT 2240 (Q88RQ5)
brenda
Bontpart, T.; Marlin, T.; Vialet, S.; Guiraud, J.L.; Pinasseau, L.; Meudec, E.; Sommerer, N.; Cheynier, V.; Terrier, N.
Two shikimate dehydrogenases, VvSDH3 and VvSDH4, are involved in gallic acid biosynthesis in grapevine
J. Exp. Bot.
67
3537-3550
2016
Vitis vinifera (A0A168S2G5), Vitis vinifera (A0A168S2H6), Vitis vinifera (A0A168S2B8), Vitis vinifera (D7TUX1)
brenda
Peek, J.; Castiglione, G.; Shi, T.; Christendat, D.
Isolation and molecular characterization of the shikimate dehydrogenase domain from the Toxoplasma gondii AROM complex
Mol. Biochem. Parasitol.
194
16-19
2014
Toxoplasma gondii
brenda
Avitia-Dominguez, C.; Sierra-Campos, E.; Salas-Pacheco, J.M.; Najera, H.; Rojo-Dominguez, A.; Cisneros-Martinez, J.; Tellez-Valencia, A.
Inhibition and biochemical characterization of methicillin-resistant Staphylococcus aureus shikimate dehydrogenase: an in silico and kinetic study
Molecules
19
4491-4509
2014
Staphylococcus aureus, Staphylococcus aureus ATCC MRSA252
brenda
Li, Z.; Liu, Y.; Bai, X.; Deng, Q.; Wang, J.; Zhang, G.; Xiao, C.; Mei, Y.; Wang, Y.
SAR studies on 1,2,4-triazolo[3,4-b][1,3,4]thiadiazoles as inhibitors of Mtb shikimate dehydrogenase for the development of novel antitubercular agents
RSC Adv.
5
97089-97101
2015
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
-
brenda
Zhang, J.; ten Pierick, A.; van Rossum, H.M.; Seifar, R.M.; Ras, C.; Daran, J.M.; Heijnen, J.J.; Wahl, S.A.
Determination of the cytosolic NADPH/NADP ratio in Saccharomyces cerevisiae using shikimate dehydrogenase as sensor reaction
Sci. Rep.
5
12846
2015
Escherichia coli (P15770)
brenda
Habashi, R.; Hacham, Y.; Dhakarey, R.; Matityahu, I.; Holland, D.; Tian, L.; Amir, R.
Elucidating the role of shikimate dehydrogenase in controlling the production of anthocyanins and hydrolysable tannins in the outer peels of pomegranate
BMC Plant Biol.
19
476
2019
Punica granatum (A0A6P8EJ47), Punica granatum
brenda
Enriquez-Mendiola, D.; Tellez-Valencia, A.; Sierra-Campos, E.; Campos-Almazan, M.; Valdez-Solana, M.; Gomez Palacio-Gastelum, M.; Avitia-Dominguez, C.
Kinetic and molecular dynamic studies of inhibitors of shikimate dehydrogenase from methicillin-resistant Staphylococcus aureus
Chem. Biol. Drug Des.
94
1504-1517
2019
Staphylococcus aureus
brenda
Li, J.; Wu, G.; Fu, Q.; Ge, H.; Liu, S.; Li, X.; Cheng, B.
Exploring the influence of conserved lysine69 on the catalytic activity of the Helicobacter pylori shikimate dehydrogenase a combined QM/MM and MD simulations
Comput. Biol. Chem.
83
107098
2019
Helicobacter pylori
brenda
Huang, K.; Li, M.; Liu, Y.; Zhu, M.; Zhao, G.; Zhou, Y.; Zhang, L.; Wu, Y.; Dai, X.; Xia, T.; Gao, L.
Functional analysis of 3-dehydroquinate dehydratase/shikimate dehydrogenases involved in shikimate pathway in Camellia sinensis
Front. Plant Sci.
10
1268
2019
Camellia sinensis (A0A3G3BK08), Camellia sinensis
brenda
Hyskova, V.; Pliskova, V.; Cerveny, V.; Ryslava, H.
NADP-dependent enzymes are involved in response to salt and hypoosmotic stress in cucumber plants
Gen. Physiol. Biophys.
36
247-258
2017
Cucumis sativus (A0A0A0LQ48)
brenda
Wang, K.; Zhu, M.; Tang, Y.; Liu, J.; Yan, F.; Yu, Z.; Zhu, J.
Integration of virtual screening and susceptibility test to discover active-site subpocket-specific biogenic inhibitors of Helicobacter pylori shikimate dehydrogenase
Int. Microbiol.
22
69-80
2019
Helicobacter pylori (Q56S04), Helicobacter pylori
brenda
Skariyachan, S.; Manjunath, M.; Bachappanavar, N.
Screening of potential lead molecules against prioritised targets of multi-drug-resistant-Acinetobacter baumannii - insights from molecular docking, molecular dynamic simulations and in vitro assays
J. Biomol. Struct. Dyn.
37
1146-1169
2019
Acinetobacter baumannii
brenda
Punkvang, A.; Kamsri, P.; Mulholland, A.; Spencer, J.; Hannongbua, S.; Pungpo, P.
Simulations of shikimate dehydrogenase from Mycobacterium tuberculosis in complex with 3-dehydroshikimate and NADPH suggest strategies for MtbSDH inhibition
J. Chem. Inf. Model.
59
1422-1433
2019
Mycobacterium tuberculosis (A0A045GU47), Mycobacterium tuberculosis, no activity in Homo sapiens
brenda
Diaz-Quiroz, D.C.; Cardona-Felix, C.S.; Viveros-Ceballos, J.L.; Reyes-Gonzalez, M.A.; Bolivar, F.; Ordonez, M.; Escalante, A.
Synthesis, biological activity and molecular modelling studies of shikimic acid derivatives as inhibitors of the shikimate dehydrogenase enzyme of Escherichia coli
J. Enzyme Inhib. Med. Chem.
33
397-404
2018
Escherichia coli (P15770), Escherichia coli
brenda
Garcia, S.; Flores, N.; De Anda, R.; Hernandez, G.; Gosset, G.; Bolivar, F.; Escalante, A.
The role of the ydiB gene, which encodes quinate/shikimate dehydrogenase, in the production of quinic, dehydroshikimic and shikimic acids in a PTS-strain of Escherichia coli
J. Mol. Microbiol. Biotechnol.
27
11-21
2017
Escherichia coli (P0A6D5), Escherichia coli PB12 (P0A6D5)
brenda
Gritsunov, A.; Peek, J.; Diaz Caballero, J.; Guttman, D.; Christendat, D.
Structural and biochemical approaches uncover multiple evolutionary trajectories of plant quinate dehydrogenases
Plant J.
95
812-822
2018
Arabidopsis thaliana (Q9SQT8)
brenda
Carrington, Y.; Guo, J.; Le, C.H.; Fillo, A.; Kwon, J.; Tran, L.T.; Ehlting, J.
Evolution of a secondary metabolic pathway from primary metabolism shikimate and quinate biosynthesis in plants
Plant J.
95
823-833
2018
Chlamydomonas reinhardtii, Physcomitrium patens, Pinus taeda, Populus trichocarpa, Rhodopirellula baltica, Selaginella moellendorffii
brenda
Tahara, K.; Nishiguchi, M.; Funke, E.; Miyazawa, S.I.; Miyama, T.; Milkowski, C.
Dehydroquinate dehydratase/shikimate dehydrogenases involved in gallate biosynthesis of the aluminum-tolerant tree species Eucalyptus camaldulensis
Planta
253
3
2020
Eucalyptus camaldulensis (A0A5H2WZU5), Eucalyptus camaldulensis (A0A5H2WVH6), Eucalyptus camaldulensis (A0A5H2X4C4), Eucalyptus camaldulensis
brenda
Garcia-Guevara, F.; Bravo, I.; Martinez-Anaya, C.; Segovia, L.
Cofactor specificity switch in shikimate dehydrogenase by rational design and consensus engineering
Protein Eng. Des. Sel.
30
533-541
2017
Escherichia coli (P15770), Escherichia coli
brenda
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