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
-
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
1.1.1.282 quinate/shikimate dehydrogenase [NAD(P)+]Advanced search results
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results (Substrates Products
Substrates Products on EC 1.1.1.282 - quinate/shikimate dehydrogenase [NAD(P)+]
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway
-
-
?
dihydroshikimate + NAD+
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
L-quinate + nicotinamide 1,N6-ethenoadenine dinucleotide
3-dehydroquinate + ?
-
69% of the activity with NAD+
-
-
?
L-quinate + nicotinamide hypoxanthine dinucleotide
3-dehydroquinate + ?
-
1.3fold higher activity than with NAD+
-
-
?
L-quinate + oxidized nicotinamide 1,N6-ethanoadenine dinucleotide
3-dehydroquinate + reduced nicotinamide 1,N6-ethanoadenine dinucleotide
-
69% activity compared to NAD+
-
-
r
quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
-
-
-
?
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate + NAD+
4-hydroxy-3-oxocyclohexane-c-1-carboxylate + NADH + H+
-
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, 44% of the activity with (-)-quinate
(-)-isomer, reverse reaction: 2.2fold higher activity than with (-)-3-dehydroquinate
-
r
t-3-hydroxy-4-oxocyclohexane-c-1-carboxylate + NAD+
?
-
6% of the activity with (-)-quinate
-
-
?
3-dehydroquinate + NADPH + H+
L-quinate + NADP+
-
may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid
-
-
?
dihydroshikimate + NAD+
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
-
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, 38% of the activity with (-)-quinate
(-)-enantiomer, reverse reaction: 3.3fold higher activity than with (-)-3-dehydroquinate
-
r
dihydroshikimate + NAD+
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
-
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, 38% of the activity with (-)-quinate
(-)-enantiomer, reverse reaction: 3.3fold higher activity than with (-)-3-dehydroquinate
-
r
L-quinate + 3-acetylpyridine adenine dinucleotide
3-dehydroquinate + ?
-
67% of the activity with NAD+
-
-
?
L-quinate + 3-acetylpyridine adenine dinucleotide
3-dehydroquinate + ?
-
67% of the activity with NAD+
-
-
?
L-quinate + beta-NAD+
3-dehydroquinate + beta-NADH + H+
-
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, a single enzyme with both quinate and shikimate dehydrogenase activity
(-)-enantiomer, reverse reaction: lower activity than with t-4,c-5-dihydroxy-3-oxocyclohexane-c-1-carboxylate or 4-hydroxy-3-oxocyclohexane-c-1-carboxylate
-
r
L-quinate + beta-NAD+
3-dehydroquinate + beta-NADH + H+
-
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, a single enzyme with both quinate and shikimate dehydrogenase activity
(-)-enantiomer, reverse reaction: lower activity than with t-4,c-5-dihydroxy-3-oxocyclohexane-c-1-carboxylate or 4-hydroxy-3-oxocyclohexane-c-1-carboxylate
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r
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
detailed strucure of YdiB, specificity for binding NAD+/NADH over NADP+/NADPH
-
-
r
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
YdiB is a dual specific quinate/shikimate dehydrogenase that utilizes either NAD+ or NADP+ as cofactor, YdiB is equally active with shikimate or quinate, but has a tendency to be more efficient with NAD+ than with NADP+, detailed structure of YdiB, mechanism
-
-
?
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
-
bifunctional enzyme with a single binding site for both substrates quinate and shikimate, the velocity is approximately 3fold lower with quinate than with shikimate
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold greater with quinate than with shikimate
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
0.3% of the activity with NAD+
-
-
?
quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
detailed strucure of YdiB, catalytic mechanism, specificity for binding NAD+/NADH over NADP+/NADPH
-
-
r
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
YdiB is a dual specific quinate/shikimate dehydrogenase that utilizes either NAD+ or NADP+ as cofactor, YdiB is equally active with shikimate or quinate, but has a tendency to be more efficient with NAD+ than with NADP+, detailed structure of YdiB, mechanism
model for 3-dehydroshikimate recognition
-
?
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
-
bifunctional enzyme with a single binding site for both substrates quinate and shikimate, the velocity is approximately 3fold higher with shikimate than with quinate
-
-
?
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, a single enzyme with both quinate and shikimate dehydrogenase activity, 72% of the activity with (-)-quinate
(-)-enantiomer, reverse reaction: 15% of the activity with (-)-3-dehydroquinate
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold lower with shikimate than with quinate
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
very low activity with NADP+
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
very low activity with NADP+
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
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
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-
?
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
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-
?
additional information
?
-
QsuD reduces 3-dehydroquinate using NADH and oxidizes quinate using NAD+ as cofactor
-
-
?
additional information
?
-
the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity
-
-
?
additional information
?
-
the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity
-
-
?
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
-
-
?
additional information
?
-
the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity
-
-
?
additional information
?
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QsuD reduces 3-dehydroquinate using NADH and oxidizes quinate using NAD+ as cofactor
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-
?
additional information
?
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-
YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source
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-
?
additional information
?
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YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source
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-
?
additional information
?
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-
the synthesis of quinate results from the reduction of 3-dehydroquinate by YdiB before its conversion to 3-dehydroshikimate. In Escherichia coli strain W3110.shik, YdiB, rather than AroE, catalyzes the oxidation of shikimate to 3-dehydroshikimate and the reduction of 3-dehydroquinate to quinate
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-
?
additional information
?
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-
the synthesis of quinate results from the reduction of 3-dehydroquinate by YdiB before its conversion to 3-dehydroshikimate. In Escherichia coli strain W3110.shik, YdiB, rather than AroE, catalyzes the oxidation of shikimate to 3-dehydroshikimate and the reduction of 3-dehydroquinate to quinate
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-
?
additional information
?
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-
catalyzes the first reaction in the inducible quinic acid catabolic pathway
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-
?
additional information
?
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NAD+-utilizing QDHs are more active with quinate than with shikimate
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-
-
additional information
?
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-
enzyme PintaQDH reacts equally well with both shikimate and quinate
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-
-
additional information
?
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-
the enzyme preferentially uses quinate as a substrate in vitro like a quinate dehydrogenase, EC 1.1.1.24, with only residual shikimate dehydrogenase, SDH, activity, cf. EC 1.1.1.25
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
-
-
?
additional information
?
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-
initial enzyme of the hydroaromatic pathway
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-
?
additional information
?
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-
substrate specificity, enzyme is highly stereospecific with regard to hydroaromatic substrates, oxidizing only the axial hydroxyl group at C-3 of (-)-enantiomer of quinate, shikimate, dihydroshikimate and t-3,t-4-dihydroxycyclohexane-c-1-carboxylate, enzyme shows activity with several NAD+ analogues, reverse reaction: not 4-hydroxy-3-oxocyclohex-4-ene-c-1-carboxylate, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide
-
-
?
additional information
?
-
-
initial enzyme of the hydroaromatic pathway
-
-
?
additional information
?
-
-
substrate specificity, enzyme is highly stereospecific with regard to hydroaromatic substrates, oxidizing only the axial hydroxyl group at C-3 of (-)-enantiomer of quinate, shikimate, dihydroshikimate and t-3,t-4-dihydroxycyclohexane-c-1-carboxylate, enzyme shows activity with several NAD+ analogues, reverse reaction: not 4-hydroxy-3-oxocyclohex-4-ene-c-1-carboxylate, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide
-
-
?
additional information
?
-
NAD+-utilizing QDHs are more active with quinate than with shikimate
-
-
-
additional information
?
-
NAD+-utilizing QDHs are more active with quinate than with shikimate
-
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-
