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Literature summary for 1.1.1.282 extracted from

  • H÷ppner, A.; Schomburg, D.; Niefind, K.
    Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination (2013), Biol. Chem., 394, 1505-1516.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme with bound NAD+ in a binary complex, and as ternary complexes with NADH plus either shikimate or quinate, sitting drop vapour diffusion method, for the ternary complexes: mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 500 mM NaCl, 20% v/v glycerol, with 1 mM NAD+/NADH or additonally with 35 mM of either quinate or shikimate, with 0.002 ml of crystallization solution containing for the QSDH-NAD+ crystals 1.6 M trisodium citrate, pH 6.5-6.9, 25-62 mM CoCl2, or for crystals of the QSDH-quinate-NADH and QSDH-shikimate-NADH 24% w/v polyethylene glycol 6000, 360-400 mM CaCl2, 100 mM Tris-HCl, pH 8.0-9.5. Crystals are soaked in a cryoprotectant containing 30% w/v polyethylene glycol 6000, 25% v/v glycerol, 100 mM Tris-HCl, pH 8.5, for 1 h, X-ray diffraction structure determination and analysis at 1.0-1.6 A resolution, structure modelling Corynebacterium glutamicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.13
-
NAD+ pH 7.5, 30┬░C, with quinate Corynebacterium glutamicum
0.28
-
NAD+ pH 9.0-9.5, 30┬░C, with quinate Corynebacterium glutamicum
0.46
-
NAD+ pH 10.0-10.5, 30┬░C, with shikimate Corynebacterium glutamicum
0.87
-
NAD+ pH 7.5, 30┬░C, with shikimate Corynebacterium glutamicum
1.56
-
L-quinate pH 7.5, 30┬░C, with NAD+ Corynebacterium glutamicum
2.38
-
L-quinate pH 9.0-9.5, 30┬░C, with NAD+ Corynebacterium glutamicum
10.16
-
shikimate pH 7.5, 30┬░C, with NAD+ Corynebacterium glutamicum
55.88
-
shikimate pH 10.0-10.5, 30┬░C, with NAD+ Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-quinate + NAD+ Corynebacterium glutamicum
-
3-dehydroquinate + NADH + H+
-
?
additional information Corynebacterium glutamicum the enzyme CglQSDH shows a substrate preference for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes ?
-
?
additional information Corynebacterium glutamicum ATCC 13032 the enzyme CglQSDH shows a substrate preference for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes ?
-
?
shikimate + NAD+ Corynebacterium glutamicum
-
3-dehydroshikimate + NADH + H+
-
?
shikimate + NAD+ Corynebacterium glutamicum ATCC 13032
-
3-dehydroshikimate + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q9X5C9
-
-
Corynebacterium glutamicum ATCC 13032 Q9X5C9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-quinate + NAD+
-
Corynebacterium glutamicum 3-dehydroquinate + NADH + H+
-
?
additional information the enzyme CglQSDH shows a substrate preference for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes Corynebacterium glutamicum ?
-
?
additional information the enzyme CglQSDH shows a substrate preference for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes Corynebacterium glutamicum ATCC 13032 ?
-
?
shikimate + NAD+
-
Corynebacterium glutamicum 3-dehydroshikimate + NADH + H+
-
?
shikimate + NAD+
-
Corynebacterium glutamicum ATCC 13032 3-dehydroshikimate + NADH + H+
-
?

Subunits

Subunits Comment Organism
More enzyme three-dimensional structure determination, analysis, and comparisons, overview. The N-terminal or catalytic domain comprises residues 1 to 113 and 256 to 283, whereas the C-terminal or nucleotide-binding domain is build up of residues 114 to 255. The catalytic domain forms an open alpha/beta sandwich, which is characteristic for enzymes of the SDH/QDH family. The substrate-binding site is located in the N-terminal domain, close to the nicotinamide ring of the cofactor Corynebacterium glutamicum

Synonyms

Synonyms Comment Organism
cgl0424
-
Corynebacterium glutamicum
QSDH
-
Corynebacterium glutamicum
qsuD
-
Corynebacterium glutamicum
quinate/shikimate dehydrogenase
-
Corynebacterium glutamicum

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
30
-
assay at Corynebacterium glutamicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
30.13
-
shikimate pH 7.5, 30┬░C, with NAD+ Corynebacterium glutamicum
43.67
-
NAD+ pH 7.5, 30┬░C, with quinate Corynebacterium glutamicum
50.82
-
L-quinate pH 7.5, 30┬░C, with NAD+ Corynebacterium glutamicum
61.12
-
NAD+ pH 7.5, 30┬░C, with shikimate Corynebacterium glutamicum
104.9
-
L-quinate pH 9.0-9.5, 30┬░C, with NAD+ Corynebacterium glutamicum
105.8
-
NAD+ pH 10.0-10.5, 30┬░C, with shikimate Corynebacterium glutamicum
214.1
-
shikimate pH 10.0-10.5, 30┬░C, with NAD+ Corynebacterium glutamicum
223.1
-
NAD+ pH 9.0-9.5, 30┬░C, with quinate Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 9.5 quinate oxidation Corynebacterium glutamicum
10 10.5 shikimate oxidation Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
additional information CglQSDH is strictly NAD(H)-dependent due to structural features Corynebacterium glutamicum
NAD+
-
Corynebacterium glutamicum
NADH
-
Corynebacterium glutamicum

General Information

General Information Comment Organism
additional information substrate binding site structure, overview. Quinate binding causes a slight closure of the N- and C-terminal domain of CglQSDH. Shikimate binding causes a alternative side-chain conformation of Lys73 Corynebacterium glutamicum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1
-
shikimate pH 7.5, 30┬░C, with NAD+ Corynebacterium glutamicum
4.24
-
shikimate pH 10.0-10.5, 30┬░C, with NAD+ Corynebacterium glutamicum
33.3
-
L-quinate pH 7.5, 30┬░C, with NAD+ Corynebacterium glutamicum
44.05
-
L-quinate pH 9.0-9.5, 30┬░C, with NAD+ Corynebacterium glutamicum
71.58
-
NAD+ pH 7.5, 30┬░C, with shikimate Corynebacterium glutamicum
329.1
-
NAD+ pH 7.5, 30┬░C, with quinate Corynebacterium glutamicum
464.7
-
NAD+ pH 10.0-10.5, 30┬░C, with shikimate Corynebacterium glutamicum
826.6
-
NAD+ pH 9.0-9.5, 30┬░C, with quinate Corynebacterium glutamicum