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Information on EC 1.1.1.282 - quinate/shikimate dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.282
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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
1.1.1.282 quinate/shikimate dehydrogenase [NAD(P)+]
IUBMB Comments
This is the second shikimate dehydrogenase enzyme found in Escherichia coli. It can use both quinate and shikimate as substrates and either NAD+ or NADP+ as acceptor. The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.282
- 3-dehydroquinate
- lignin
-
corynebacterium
-
nad+-dependent
- glutamicum
-
cosubstrate
- drug development
- dehydrogenases
- agriculture
- synthesis
- medicine
- pharmacology
Reaction Schemes
showSynonyms
rifi2, sdh/qdh, quinate/shikimate 5-dehydrogenase, shikimate/quinate dehydrogenase, poptr2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cgR_0495
NAD+-dependent enzyme quinate/shikimate dehydrogenase
QDH
QSDH
qsuD
quinate dehydrogenase
quinate/shikimate dehydrogenase
RifI2
SDH/QDH
shikimate/quinate dehydrogenase
YdiB
additional information
quinate/shikimate dehydrogenase
-
-
ambiguous
-
YdiB
-
-
-
-
additional information
YdiB is a class A NAD(P)+-dependent oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
stereospecificity
-
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
reaction mechanism
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
reaction mechanism, in which an aspartate acts as the general acid/base catalyst during the hydride transfer
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
catalytic reaction mechanism
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
(1)
-
-
-
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
catalytic reaction mechanism
-
-
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
stereospecificity
-
-
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
stereospecificity
-
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
reaction mechanism
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
reaction mechanism, in which an aspartate acts as the general acid/base catalyst during the hydride transfer
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
catalytic reaction mechanism
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
(2)
-
-
-
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
catalytic reaction mechanism
-
-
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
stereospecificity
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
quinate degradation II
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SYSTEMATIC NAME
IUBMB Comments
L-quinate:NAD(P)+ 3-oxidoreductase
This is the second shikimate dehydrogenase enzyme found in Escherichia coli. It can use both quinate and shikimate as substrates and either NAD+ or NADP+ as acceptor. The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
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CAS REGISTRY NUMBER
COMMENTARY
9026-87-3
cf. EC 1.1.1.25
9028-28-8
cf. EC 1.1.1.24
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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 + NAD(P)H + H+
shikimate + NAD(P)+
Substrates: YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway
Products: -
Products: -
?
3-dehydroshikimate + NADH + H+
shikimate + NAD+
Substrates: -
Products: -
Products: -
r
dihydroshikimate + NAD+
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
L-quinate + 3-acetylpyridine adenine dinucleotide
3-dehydroquinate + ?
-
Substrates: 67% of the activity with NAD+
Products: -
Products: -
?
L-quinate + nicotinamide 1,N6-ethenoadenine dinucleotide
3-dehydroquinate + ?
-
Substrates: 69% of the activity with NAD+
Products: -
Products: -
?
L-quinate + nicotinamide hypoxanthine dinucleotide
3-dehydroquinate + ?
-
Substrates: 1.3fold higher activity than with NAD+
Products: -
Products: -
?
L-quinate + oxidized nicotinamide 1,N6-ethanoadenine dinucleotide
3-dehydroquinate + reduced nicotinamide 1,N6-ethanoadenine dinucleotide
-
Substrates: 69% activity compared to NAD+
Products: -
Products: -
r
quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate + NAD+
4-hydroxy-3-oxocyclohexane-c-1-carboxylate + NADH + H+
t-3-hydroxy-4-oxocyclohexane-c-1-carboxylate + NAD+
?
-
Substrates: 6% of the activity with (-)-quinate
Products: -
Products: -
?
3-dehydroquinate + NADPH + H+
L-quinate + NADP+
Substrates: -
Products: -
Products: -
r
3-dehydroquinate + NADPH + H+
L-quinate + NADP+
-
Substrates: may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid
Products: -
Products: -
?
dihydroshikimate + NAD+
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
-
Substrates: 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
Products: (-)-enantiomer, reverse reaction: 3.3fold higher activity than with (-)-3-dehydroquinate
Products: (-)-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+
-
Substrates: 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
Products: (-)-enantiomer, reverse reaction: 3.3fold higher activity than with (-)-3-dehydroquinate
Products: (-)-enantiomer, reverse reaction: 3.3fold higher activity than with (-)-3-dehydroquinate
r
L-quinate + beta-NAD+
3-dehydroquinate + beta-NADH + H+
-
Substrates: 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
Products: (-)-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
Products: (-)-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+
-
Substrates: 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
Products: (-)-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
Products: (-)-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 + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
Substrates: 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
Products: -
Products: -
?
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
Substrates: detailed strucure of YdiB, specificity for binding NAD+/NADH over NADP+/NADPH
Products: -
Products: -
r
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
-
Substrates: bifunctional enzyme with a single binding site for both substrates quinate and shikimate, the velocity is approximately 3fold lower with quinate than with shikimate
Products: -
Products: -
?
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
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
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
Substrates: 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
Products: -
Products: -
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
Substrates: 0.3% of the activity with NAD+
Products: -
Products: -
?
quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
Substrates: 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
Products: model for 3-dehydroshikimate recognition
Products: model for 3-dehydroshikimate recognition
?
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
Substrates: detailed strucure of YdiB, catalytic mechanism, specificity for binding NAD+/NADH over NADP+/NADPH
Products: -
Products: -
r
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
-
Substrates: bifunctional enzyme with a single binding site for both substrates quinate and shikimate, the velocity is approximately 3fold higher with shikimate than with quinate
Products: -
Products: -
?
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
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: -
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: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: 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
Products: (-)-enantiomer, reverse reaction: 15% of the activity with (-)-3-dehydroquinate
Products: (-)-enantiomer, reverse reaction: 15% of the activity with (-)-3-dehydroquinate
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: 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
Products: (-)-enantiomer, reverse reaction: 15% of the activity with (-)-3-dehydroquinate
Products: (-)-enantiomer, reverse reaction: 15% of the activity with (-)-3-dehydroquinate
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 + 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: 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
Products: -
Products: -
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: very low activity with NADP+
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: very low activity with NADP+
Products: -
Products: -
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Substrates: -
Products: -
Products: -
r
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate + NAD+
4-hydroxy-3-oxocyclohexane-c-1-carboxylate + NADH + H+
-
Substrates: 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
Products: (-)-isomer, reverse reaction: 2.2fold higher activity than with (-)-3-dehydroquinate
Products: (-)-isomer, reverse reaction: 2.2fold higher activity than with (-)-3-dehydroquinate
r
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate + NAD+
4-hydroxy-3-oxocyclohexane-c-1-carboxylate + NADH + H+
-
Substrates: 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
Products: (-)-isomer, reverse reaction: 2.2fold higher activity than with (-)-3-dehydroquinate
Products: (-)-isomer, reverse reaction: 2.2fold higher activity than with (-)-3-dehydroquinate
r
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: QsuD reduces 3-dehydroquinate using NADH and oxidizes quinate using NAD+ as cofactor
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source
Products: -
Products: -
?
additional information
?
-
Substrates: YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in quinic acid metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes the first reaction in the inducible quinic acid catabolic pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: NAD+-utilizing QDHs are more active with quinate than with shikimate
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in quinic acid metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme PintaQDH reacts equally well with both shikimate and quinate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
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: 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: initial enzyme of the hydroaromatic pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: initial enzyme of the hydroaromatic pathway
Products: -
Products: -
?
additional information
?
-
Substrates: NAD+-utilizing QDHs are more active with quinate than with shikimate
Products: -
Products: -
?
additional information
?
-
Substrates: NAD+-utilizing QDHs are more active with quinate than with shikimate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-dehydroquinate + NADPH + H+
L-quinate + NADP+
-
Substrates: may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid
Products: -
Products: -
?
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
Substrates: YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: -
Products: -
Products: -
r
quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
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: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: -
Products: -
Products: -
?
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
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source
Products: -
Products: -
?
additional information
?
-
Substrates: YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in quinic acid metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes the first reaction in the inducible quinic acid catabolic pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in quinic acid metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: initial enzyme of the hydroaromatic pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: initial enzyme of the hydroaromatic pathway
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
-
67% of the activity with NAD+
nicotinamide 1,N6-ethenoadenine dinucleotide
-
69% of the activity with NAD+
nicotinamide hypoxanthine dinucleotide
-
1.3fold higher activity than with NAD+
NAD+
utilizes either NAD+ or NADP+ as a cofactor, tendency to be more efficient with NAD+ than with NADP+, mode of binding
NAD+
NAD+ binding site, bound very tightly, NAD+ is bound to the Rossmann domain in an elongated fashion with the nicotinamide ring in the pro-R conformation, specificity for binding NAD+ over NADP+
NAD+
the C-terminal domain of each protomer in the RifI2 asymmetric unit contains a bound molecule of NAD+, Cofactor binding structure and mechanism, detailed overview
NADP+
utilizes either NAD+ or NADP+ as a cofactor, tendency to be more efficient with NAD+ than with NADP+, mode of binding
additional information
-
absolute requirement for a nicotinamide nucleotide cofactor for the oxidation of quinate or shikimate, cofactor specificity, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide
-
additional information
the turnover number is lower with NADP+ instead of NAD+ as cofactor. NADP(H) is just only for 3-dehydroquinate reduction by the enzyme
-
additional information
CglQSDH is strictly NAD(H)-dependent due to structural features
-
additional information
-
CglQSDH is strictly NAD(H)-dependent due to structural features
-
additional information
in the RifI2 structure, the NADP+-specifying motif is replaced with Asp-Pro-Ser-Thr-Ala-Arg (residues 156-161). The side chain of Asp156 binds to the adenine ribose of NAD+, while its negative charge is predicted to repel the additional phosphate of NADP+. RifI2 possesses low apparent binding affinity for NADP+. Analysis of the cofactor-binding sites of the RifI2NAD+ complex and structure comparison, inportance of the invariant residue Asn193 in the cofactor-binding site, overview
-
additional information
-
in the RifI2 structure, the NADP+-specifying motif is replaced with Asp-Pro-Ser-Thr-Ala-Arg (residues 156-161). The side chain of Asp156 binds to the adenine ribose of NAD+, while its negative charge is predicted to repel the additional phosphate of NADP+. RifI2 possesses low apparent binding affinity for NADP+. Analysis of the cofactor-binding sites of the RifI2NAD+ complex and structure comparison, inportance of the invariant residue Asn193 in the cofactor-binding site, overview
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
divalent cations are not required for the activity of RifI2, as the reaction rate is not altered in the presence of 5 mM Ca2+, Mg2+, Mn2+, or Zn2+. Similarly, the reaction is not affected by the addition of 10 mM EDTA to chelate any endogenous divalent cations associated with the enzyme
additional information
-
divalent cations are not required for the activity of RifI2, as the reaction rate is not altered in the presence of 5 mM Ca2+, Mg2+, Mn2+, or Zn2+. Similarly, the reaction is not affected by the addition of 10 mM EDTA to chelate any endogenous divalent cations associated with the enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.65
3-acetylpyridine adenine dinucleotide
-
pH 10, cosubstrate (-)-quinate
0.005 - 0.012
NADPH
-
pH 10, 20°C, cosubstrate dehydroquinate, both forms of quinate (shikimate) dehydrogenase
0.48
nicotinamide hypoxanthine dinucleotide
-
pH 10, cosubstrate (-)-quinate
0.51
oxidized nicotinamide 1,N6-ethanoadenine dinucleotide
-
pH 10, cosubstrate (-)-quinate
-
2.47
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate
-
pH 10, (-)-enantiomer, cosubstrate NAD+
0.42
3-dehydroquinate
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
dehydroquinate
-
pH 10, 20°C, cosubstrate NADPH, form P1 of quinate (shikimate) dehydrogenase
5.3
dehydroquinate
-
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
-
pH and temperature not specified in the publication, enzyme PintaQDH with NADP+
3.4 - 3.6
L-quinate
-
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
NADP+
-
pH 10, 20°C, cosubstrate shikimate, both forms of quinate (shikimate) dehydrogenase
0.007
NADP+
-
pH 10, 20°C, cosubstrate L-quinate, both forms of quinate (shikimate) dehydrogenase
0.219
NADP+
-
with quinate, pH and temperature not specified in the publication
0.271
NADP+
-
with shikimate, pH and temperature not specified in the publication
0.438
NADP+
-
with quinate, pH and temperature not specified in the publication
0.487
NADP+
-
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
quinate
-
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
-
with NAD+, pH and temperature not specified in the publication
0.7 - 0.8
shikimate
-
pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase
0.82
shikimate
-
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
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis constant with quinate as substrate is lower than that with shikimate under optimal conditions
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.31
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH
114
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
5.67
3-dehydroshikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
14.6
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
0.105
NAD+
wild type enzyme, in the presence of shikimate, 20°C, pH 9.0
0.142
NAD+
wild type enzyme, in the presence of L-quinate, 20°C, pH 9.0
0.74
NAD+
with shikimate, pH and temperature not specified in the publication
3.8
NAD+
-
with shikimate, pH and temperature not specified in the publication
10.5
NAD+
with quinate, pH and temperature not specified in the publication
20.8
NAD+
-
with quinate, pH and temperature not specified in the publication
0.0018
NADP+
-
with quinate, pH and temperature not specified in the publication
0.335
NADP+
-
with shikimate, pH and temperature not specified in the publication
8.6
NADP+
-
with shikimate, pH and temperature not specified in the publication
9.4
quinate
with NAD+, pH and temperature not specified in the publication
16.2
quinate
-
with NAD+, pH and temperature not specified in the publication
1.75
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.96
3-dehydroshikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
8.16
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH
271.4
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
32.88
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
1.43
NAD+
with shikimate, pH and temperature not specified in the publication
12.1
NAD+
-
with shikimate, pH and temperature not specified in the publication
16.5
NAD+
with quinate, pH and temperature not specified in the publication
36.8
NAD+
-
with quinate, pH and temperature not specified in the publication
0.008
NADP+
-
with quinate, pH and temperature not specified in the publication
0.688
NADP+
-
with shikimate, pH and temperature not specified in the publication
15.98
NADP+
-
with quinate, pH and temperature not specified in the publication
31.73
NADP+
-
with shikimate, pH and temperature not specified in the publication
44.97
quinate
-
with NAD+, pH and temperature not specified in the publication
50.8
quinate
with NAD+, pH and temperature not specified in the publication
151.4
quinate
-
with NAD+, pH and temperature not specified in the publication
1.35
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00391
-
hypocotyls of 20 days old saplings, quinate and NADP+ as substrates
0.0664
-
needles, in June, the period of maximal quinate dehydrogenase content, quinate and NADP+ as substrates
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
-
oxidation reaction, quinate or shikimate as substrates, 50 mM glycine-KOH
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
-
the rate of activity decreases more rapidly, maximal 25% at pH 7.5, at pH values from 8.5 to 7 when shikimate rather than quinate is used as substrate
additional information
the catalytic reaction of QsuD is highly susceptible to pH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
trees grown in a field at the University of Victoria
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
from current-year shoots of 20 years old trees, the youngest basal parts of needles
brenda
-
Poptr2 and Poptr3 are highly expressed in roots and root tips, respectively
brenda
-
Poptr3 is highly expressed in bark and some vascular tissues
brenda
additional information
-
Poptr4 shows a distinct expression pattern with predominant expression in leaves, seedlings, and stomata and some expression in bark and differentiating tissues. Isozyme expression profiles, overview
brenda
additional information
the gene for the NAD+-dependent enzyme shows higher expression in the roots in the later stages of Solanum lycopersicum fruit development and especially during fruit ripening. Unique expression profiles imply that QDH genes for NAD+- and NADP+-specific enzymes, gene expression analysis
brenda
additional information
the gene for the NAD+-dependent enzyme shows higher expression in the roots in the later stages of Solanum lycopersicum fruit development and especially during fruit ripening. Unique expression profiles imply that QDH genes for NAD+- and NADP+-specific enzymes, gene expression analysis
brenda
additional information
the NADP+-specific enzyme shows higher expression levels in green tissues, including leaves, green stems and flowers and during the early stages of fruit development, gene expression analysis. The unique expression profiles imply that QDH genes for NAD+- and NADP+-specific enzymes are likely to have distinct physiological roles
brenda
additional information
the NADP+-specific enzyme shows higher expression levels in green tissues, including leaves, green stems and flowers and during the early stages of fruit development, gene expression analysis. The unique expression profiles imply that QDH genes for NAD+- and NADP+-specific enzymes are likely to have distinct physiological roles
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the NADP+-specific DHQD-QDH from this plant contains a predicted chloroplast-targeting 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
-
members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. Plant SDHs are generally more similar to bacterial SDH/QDH YdiB (25-30% similarity) than to bacterial SDH AroE (21-28%)
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
-
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
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
-
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
-
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
-
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
-
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
-
malfunction
disruption of the qdh gene in prevents growth on both compounds, demonstrating the important role of the enzyme in hydroaromatic catabolism
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
-
disruption of the qdh gene in prevents growth on both compounds, demonstrating the important role of the enzyme in hydroaromatic catabolism
-
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
-
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
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 enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
-
physiological function
-
quinate and its derivatives are protective secondary metabolites, quinate is an astringent feeding deterrent that can be formed in a single step reaction from 3-dehydroquinate catalyzed by quinate dehydrogenase
physiological function
QsuD is essential for growth on shikimate and quinate as sole carbon sources, suggesting that it is the key enzyme for shikimate/quinate utilization
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 reduced efficiency of Corynebacterium glutamicum enzyme with shikimate as a substrate may also result in part from the flexibility of the catalytic group, Lys73, which adopts multiple conformations in the shikimate-liganded enzyme structure
physiological function
-
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
physiological function
-
inactivation of ydiB results in a 75% decrease in the molar yield of quinic acid and a 6.17% reduction in the yield of quinic acid (mol/mol) relative to shikimic acid with respect to the parental strain. The overexpression of ydiB causes a 500% increase in the molar yield of quinic acid and results in a 152% increase in quinic acid (mol/mol) relative to shikimic acid, with a sharp decrease in shikimic acid production
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 reduced efficiency of Corynebacterium glutamicum enzyme with shikimate as a substrate may also result in part from the flexibility of the catalytic group, Lys73, which adopts multiple conformations in the shikimate-liganded enzyme structure
-
physiological function
-
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
-
physiological function
-
inactivation of ydiB results in a 75% decrease in the molar yield of quinic acid and a 6.17% reduction in the yield of quinic acid (mol/mol) relative to shikimic acid with respect to the parental strain. The overexpression of ydiB causes a 500% increase in the molar yield of quinic acid and results in a 152% increase in quinic acid (mol/mol) relative to shikimic acid, with a sharp decrease in shikimic acid production
-
physiological function
-
QsuD is essential for growth on shikimate and quinate as sole carbon sources, suggesting that it is the key enzyme for shikimate/quinate utilization
-
physiological function
-
quinate and its derivatives are protective secondary metabolites, quinate is an astringent feeding deterrent that can be formed in a single step reaction from 3-dehydroquinate catalyzed by quinate dehydrogenase
-
additional information
-
the enzymes have Gly residues instead of Ser residues in the active sites. The Ser-to-Gly conversion ompared to SDHs may generate extra space in the inferred Poptr isozymes active sites that can accommodate the hydroxyl group at the C1 position of quinate
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
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
additional information
enzyme RifI2 lacks a conserved C-terminal alpha-helix
additional information
-
enzyme RifI2 lacks a conserved C-terminal alpha-helix
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
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
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
-
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
-
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
-
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
-
additional information
-
enzyme RifI2 lacks a conserved C-terminal alpha-helix
-
Show AA Sequence and Transmembrane Helices (458 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
-
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration
53000
-
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
dimer
distinct mode of dimerization in which the individual molecules interact in a back-to-front manner, overview. The molecules of the RifI2 dimer associate via hydrophobic interactions between residues on alpha-helix alpha8 of the first molecule and alpha10' of the second molecule. In addition, the side chain of Gln167 on apha-helix alpha8 forms a hydrogen bond with the guanidinium group of Arg243' on beta-strand beta10'. A second hydrogen bond to Arg243' may be made by Asn171. Asp53 and Arg56 on alpha-helix alpha2 bind the imidazole ring of His31' on alpha-helix alpha1'
dimer
-
distinct mode of dimerization in which the individual molecules interact in a back-to-front manner, overview. The molecules of the RifI2 dimer associate via hydrophobic interactions between residues on alpha-helix alpha8 of the first molecule and alpha10' of the second molecule. In addition, the side chain of Gln167 on apha-helix alpha8 forms a hydrogen bond with the guanidinium group of Arg243' on beta-strand beta10'. A second hydrogen bond to Arg243' may be made by Asn171. Asp53 and Arg56 on alpha-helix alpha2 bind the imidazole ring of His31' on alpha-helix alpha1'
-
additional information
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
additional information
-
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
additional information
-
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of binary and ternary complexes of enzyme and substrates, PDB IDs 3JYP, 2NLO, 3JYO, and 3JYQ
crystal structure determination as enzyme in binary complex with NAD+ (PDB ID 3JYO), or in ternary complex with shikimate and NADH (PDB ID 3JYQ), or in ternary complex with quinate and NADH (PDB ID 3JYP)
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
RifI2 X-ray diffraction structure determination and analysis at 2.15 A resolution, modelling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S67A
site-directed mutagenesis, increased activity compared to wild type enzyme
N193Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N193S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N193Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
N193S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
additional information
additional information
construction of a gene qsuD deletion mutant. Cell cultures of the qsuD-deficient strain in glucose-containing medium are light yellow, whereas those of the wild-type in shikimate or quinate-containing medium are brown
additional information
-
construction of a gene qsuD deletion mutant. Cell cultures of the qsuD-deficient strain in glucose-containing medium are light yellow, whereas those of the wild-type in shikimate or quinate-containing medium are brown
-
additional information
-
ydiB-encoded enzyme knockout in Escherichia coli strain PB12
additional information
-
ydiB-encoded enzyme knockout in Escherichia coli strain PB12
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the thermal stability of enzyme is greatly enhanced by low concentrations of quinate, shikimate, NADH or high ionic strength
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM Tris-HCl buffer, pH 7.5, 500 mM NaCl, 5% glycerol
4°C, 10 mM TrisHCl buffer, pH 7.5, 500 mM NaCl, 5% glycerol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3000fold, two forms of the bifunctional quinate (shikimate) dehydrogenase: P1 and P2
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by nickel-nitrilotriacetic acid affinity chromatography
recombinant His6-tagged isozymes from Escherichia coli strain M15 by nickel affinity chromatography
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recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 gold by nickel affinity chromatography, dialysis, tag cleavage through TEV protease and removal by nickel affinity chromatography, followed by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 expression analysis, phylogenetic analysis
gene ydiB, the ydiB gene s 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
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recombinant expression of His6-tagged isozymes in Escherichia coli strain M15
-
recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 gold
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
qsuD mRNA expression is upregulated in shikimate-grown cells relative to that in the glucose-grown cells
qsuD mRNA expression is upregulated in shikimate-grown cells relative to that in the glucose-grown cells
qsuD mRNA expression is upregulated in shikimate-grown cells relative to that in the glucose-grown cells
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
pharmacology
enzymes of the shikimate pathway has been promoted as a target for the development of antimicrobial 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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barea, J.L.; Giles, N.H.
Purification and characterization of quinate (shikimate) dehydrogenase, an enzyme in the inducible quinic acid catabolic pathway of Neurospora crassa
Biochim. Biophys. Acta
524
1-14
1978
Neurospora crassa
brenda
Michel, G.; Roszak, A.W.; Sauv, V.; Maclean, J.; Matte, A.; Coggins, J.R.; Cygler, M.; Lapthorn, A.J.
Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common structural framework for different activitie
J. Biol. Chem.
278
19463-19472
2003
Escherichia coli, Escherichia coli (P0A6D5)
brenda
Benach, J.; Lee, I.; Edstrom, W.; Kuzin, A.P.; Chiang, Y.; Acton, T.B.; Montelione, G.T.; Hunt, J.F.
The 2.3- crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase
J. Biol. Chem.
278
19176-19182
2003
Escherichia coli (P0A6D5)
brenda
Bruce, N.C.; Cain, R.B.
Hydroaromatic metabolism in Rhodococcus rhodochrous: purification and characterization of its NAD-dependent quinate dehydrogenase
Arch. Microbiol.
154
179-186
1990
Rhodococcus rhodochrous, Rhodococcus rhodochrous N75
-
brenda
Osipov, V.I.; Shein, I.V.
The role of quinate dehydrogenase in quinic acid metabolism in coniferous plants
Biokhimiya
51
230-236
1986
Larix sibirica, Pinus sylvestris
-
brenda
Lindner, H.A.; Nadeau, G.; Matte, A.; Michel, G.; Menard, R.; Cygler, M.
Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli
J. Biol. Chem.
280
7162-7169
2005
Escherichia coli (P0A6D5), Escherichia coli
brenda
Ossipov, V.; Bonner, C.; Ossipova, S.; Jensen, R.
Broad-specificity quinate (shikimate) dehydrogenase from Pinus taeda needles
Plant Physiol. Biochem.
38
923-928
2000
Pinus taeda
-
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
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
Enterococcus faecium, Listeria monocytogenes, Haemophilus influenzae (P44774), Escherichia coli (P0A6D5), Shigella flexneri, Salmonella enterica subsp. enterica serovar Typhimurium, Lactiplantibacillus plantarum, Streptococcus pyogenes, Enterococcus faecalis
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 KT2440 (Q88K85), Pseudomonas putida KT2440 (Q88JP1), Pseudomonas putida KT2440 (Q88GF6)
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 (A4QB65)
brenda
Hppner, 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
Biol. Chem.
394
1505-1516
2013
Corynebacterium glutamicum (Q9X5C9), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q9X5C9)
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
Corynebacterium glutamicum (Q9X5C9), Corynebacterium glutamicum (A4QB65), Corynebacterium glutamicum ATCC 13032 (Q9X5C9)
brenda
Peek, J.; Garcia, C.; Lee, J.; Christendat, D.
Insights into the function of RifI2: structural and biochemical investigation of a new shikimate dehydrogenase family protein
Biochim. Biophys. Acta
1834
516-523
2013
Pseudomonas putida (Q88JP1), Pseudomonas putida, Pseudomonas putida KT 2240 (Q88JP1)
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
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, Escherichia coli PB12
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
Solanum lycopersicum (A0A3Q7IET9), Solanum lycopersicum (A0A3Q7H2B2), Nicotiana tabacum, Brassica napus, Brassica rapa
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
Pinus taeda
brenda
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