1.1.1.282: quinate/shikimate dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about quinate/shikimate dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.1.1.282
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1.1.1.282
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3-dehydroquinate
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lignin
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corynebacterium
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nad+-dependent
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glutamicum
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cosubstrate
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drug development
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dehydrogenases
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agriculture
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synthesis
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medicine
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pharmacology
- 1.1.1.282
- 3-dehydroquinate
- lignin
-
corynebacterium
-
nad+-dependent
- glutamicum
-
cosubstrate
- drug development
- dehydrogenases
- agriculture
- synthesis
- medicine
- pharmacology
Reaction
Synonyms
cgl0424, cgR_0495, dehydroquinate dehydratase-shikimate dehydrogenase, More, NAD+ cofactor-specific QDH, NAD+-dependent enzyme quinate/shikimate dehydrogenase, NADP+ cofactor-specific QDH, NADP+-specific DHQD-QDH, PintaQDH, Poptr2, Poptr3, Poptr4, QDH, QSDH, qsuD, quinate dehydrogenase, quinate/shikimate 5-dehydrogenase, quinate/shikimate dehydrogenase, rifI, RifI2, SDH, SDH/QDH, sdhL, shikimate/quinate dehydrogenase, YdiB
ECTree
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KM Value
KM Value on EC 1.1.1.282 - quinate/shikimate dehydrogenase [NAD(P)+]
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0.65
3-acetylpyridine adenine dinucleotide
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pH 10, cosubstrate (-)-quinate
0.005 - 0.012
NADPH
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pH 10, 20°C, cosubstrate dehydroquinate, both forms of quinate (shikimate) dehydrogenase
0.48
nicotinamide hypoxanthine dinucleotide
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pH 10, cosubstrate (-)-quinate
0.51
oxidized nicotinamide 1,N6-ethanoadenine dinucleotide
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pH 10, cosubstrate (-)-quinate
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2.47
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate
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pH 10, (-)-enantiomer, cosubstrate NAD+
0.42
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
1.141
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH
5.933
3-dehydroshikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
1
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pH 10, 20°C, cosubstrate NADPH, form P1 of quinate (shikimate) dehydrogenase
5.3
dehydroquinate
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pH 10, 20°C, cosubstrate NADPH, form P2 of quinate (shikimate) dehydrogenase
0.444
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
0.677
L-quinate
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pH and temperature not specified in the publication, enzyme PintaQDH with NADP+
3.4 - 3.6
L-quinate
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pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase
0.0122
NAD+
wild type enzyme, in the presence of shikimate, 20°C, pH 9.0
0.0158
NAD+
mutant T106A, in the presence of shihikimat, 20°C, pH 9.0
0.0184
NAD+
wild type enzyme, in the presence of L-quinate, 20°C, pH 9.0
0.314
NAD+
-
with shikimate, pH and temperature not specified in the publication
0.519
NAD+
with shikimate, pH and temperature not specified in the publication
0.565
NAD+
-
with quinate, pH and temperature not specified in the publication
0.635
NAD+
with quinate, pH and temperature not specified in the publication
0.001
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pH 10, 20°C, cosubstrate shikimate, both forms of quinate (shikimate) dehydrogenase
0.007
NADP+
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pH 10, 20°C, cosubstrate L-quinate, both forms of quinate (shikimate) dehydrogenase
0.219
NADP+
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with quinate, pH and temperature not specified in the publication
0.271
NADP+
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with shikimate, pH and temperature not specified in the publication
0.438
NADP+
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with quinate, pH and temperature not specified in the publication
0.487
NADP+
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with shikimate, pH and temperature not specified in the publication
0.519
NADP+
with shikimate, pH and temperature not specified in the publication
0.635
NADP+
with quinate, pH and temperature not specified in the publication
0.107
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with NAD+, pH and temperature not specified in the publication
0.185
quinate
with NAD+, pH and temperature not specified in the publication
0.185
quinate
with NADP+, pH and temperature not specified in the publication
0.189
quinate
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with NAD+, pH and temperature not specified in the publication
0.7 - 0.8
shikimate
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pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase
0.82
shikimate
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pH and temperature not specified in the publication, enzyme PintaQDH with NADP+
1.299
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis constant with quinate as substrate is lower than that with shikimate under optimal conditions
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