HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.1.1.282 - quinate/shikimate dehydrogenase
for references in articles please use BRENDA:EC1.1.1.282Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.282 quinate/shikimate dehydrogenaseIUBMB Comments
This is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from EC 1.1.1.25, shikimate dehydrogenase, in that it can use both quinate and shikimate as substrate and either NAD+ or NADP+ as acceptor.
Specify your search results
Word Map
- 1.1.1.282
- 3-dehydroquinate
- glutamicum
-
nad+-dependent
-
corynebacterium
- nad+
- dehydrogenases
-
hydroaromatic
-
cosubstrate
- dehydratase
- protocatechuate
- lignin
- drug development
- herbicides
- dehydroshikimate
- agriculture
- medicine
- pharmacology
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
quinate/shikimate dehydrogenase, rifi2, sdh/qdh, poptr2, quinate/shikimate 5-dehydrogenase, shikimate/quinate dehydrogenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cgR_0495
qsuD
quinate/shikimate dehydrogenase
RifI2
SDH/QDH
shikimate/quinate dehydrogenase
YdiB
additional information
YdiB is a class A NAD(P)+-dependent oxidoreductase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
reaction mechanism
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
This is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from EC 1.1.1.25, shikimate 3-dehydrogenase, in that it can use both quinate and shikimate as substrate and either NAD+ or NADP+ as acceptor
-
-
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+
stereospecificity
-
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
catalytic reaction mechanism
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+
reaction mechanism
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
This is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from EC 1.1.1.25, shikimate 3-dehydrogenase, in that it can use both quinate and shikimate as substrate and either NAD+ or NADP+ as acceptor
-
-
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+
stereospecificity
-
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
catalytic reaction mechanism
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
catalytic reaction mechanism
-
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
stereospecificity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-quinate:NAD(P)+ 3-oxidoreductase
This is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from EC 1.1.1.25, shikimate dehydrogenase, in that it can use both quinate and shikimate as substrate and either NAD+ or NADP+ as acceptor.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9026-87-3
cf. EC 1.1.1.25
9028-28-8
cf. EC 1.1.1.24
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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+
4-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+
-
?
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 + 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+
-
?
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 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
?
-
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
?
-
-
QsuD reduces 3-dehydroquinate using NADH and oxidizes quinate using NAD+ as cofactor
-
?
additional information
?
-
-
YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source
-
?
additional information
?
-
YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
catalyzes the first reaction in the inducible quinic acid catabolic pathway
-
?
additional information
?
-
-
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
-
?
additional information
?
-
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
?
-
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
?
-
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
?
-
-
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
?
-
-
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
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-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
-
-
?
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway
-
-
?
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
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+
-
-
-
-
?
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 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 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
?
-
-
YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source
-
-
?
additional information
?
-
YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
catalyzes the first reaction in the inducible quinic acid catabolic pathway
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
initial enzyme of the hydroaromatic pathway
-
-
?
additional information
?
-
-
initial enzyme of the hydroaromatic pathway
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
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+
utilizes either NAD+ or NADP+ as a cofactor, tendency to be more efficient with NAD+ than with NADP+, mode of binding
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
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 RifI2–NAD+ 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 RifI2–NAD+ complex and structure comparison, inportance of the invariant residue Asn193 in the cofactor-binding site, overview
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
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
0.001
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
0.7 - 0.8
shikimate
-
pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1.75
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.96
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+
1.35
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
-
oxidation reaction, quinate or shikimate as substrates, 50 mM glycine-KOH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
trees grown in a field at the University of Victoria
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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
-
from current-year shoots of 20 years old trees, the youngest basal parts of needles
brenda
Please 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
-
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
malfunction
disruption of the qdh gene in prevents growth on both compounds, demonstrating the important role of the enzyme in hydroaromatic catabolism
malfunction
-
disruption of the qdh gene in prevents growth on both compounds, demonstrating the important role of the enzyme in hydroaromatic catabolism
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
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
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
-
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
-
QsuD is essential for growth on shikimate and quinate as sole carbon sources, suggesting that it is the key enzyme for shikimate/quinate utilization
additional information
enzyme RifI2 lacks a conserved C-terminal alpha-helix
additional information
-
enzyme RifI2 lacks a conserved C-terminal alpha-helix
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
-
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
-
enzyme RifI2 lacks a conserved C-terminal alpha-helix
Show AA Sequence and Transmembrane Helices (1045 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
construction of an enzyme ydiB- knockout mutant JM101 strain. Fermentation processes for the production of shikimate in overproducing strains of Escherichia coli result in the simultaneous synthesis of quinic acid and 3-dehydroshikimic acid. The production of high amounts of these byproducts significantly reduces the yield of shikimate, and more importantly, the presence of quinate impairs the efficiency of shikimate extraction from supernatant cultures, reducing its purity and increasing downstream processing costs. The inactivation of the ydiB gene increases the molar proportion of shikimate and 3-dehydroshikimate with respect to quinate, showing a molar ratio of 0.81/0.05/0.14 (mol/mol/mol) of shikimate/quinate/3-dehydroshikimate. In this derivative strain, quinate production is 6.17% relative to shikimate (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce quinate production below 10% (mol/mol) relative to ahkimate in culture fermentations for shikimate production
additional information
-
construction of an enzyme ydiB- knockout mutant JM101 strain. Fermentation processes for the production of shikimate in overproducing strains of Escherichia coli result in the simultaneous synthesis of quinic acid and 3-dehydroshikimic acid. The production of high amounts of these byproducts significantly reduces the yield of shikimate, and more importantly, the presence of quinate impairs the efficiency of shikimate extraction from supernatant cultures, reducing its purity and increasing downstream processing costs. The inactivation of the ydiB gene increases the molar proportion of shikimate and 3-dehydroshikimate with respect to quinate, showing a molar ratio of 0.81/0.05/0.14 (mol/mol/mol) of shikimate/quinate/3-dehydroshikimate. In this derivative strain, quinate production is 6.17% relative to shikimate (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce quinate production below 10% (mol/mol) relative to ahkimate in culture fermentations for shikimate production
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM Tris-HCl buffer, pH 7.5, 500 mM NaCl, 5% glycerol
4°C, 10 mM Tris–HCl buffer, pH 7.5, 500 mM NaCl, 5% glycerol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3000fold, two forms of the bifunctional quinate (shikimate) dehydrogenase: P1 and P2
-
by nickel-nitrilotriacetic acid affinity chromatography
recombinant His6-tagged isozymes from Escherichia coli strain M15 by nickel affinity chromatography
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 ydiB, recombinant overexpression in Escherichia coli strain PB12 causing a 500% increase in the molar yield of quinate and results in a 152% increase in quinate (mol/mol) relative to shikimate, with a sharp decrease in shikimate production. Transcriptomic analysis of PB12.SA22 and ydiB derivative strains
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
synthesis
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
synthesis
-
enzyme YdiB displays a clear activity on quinate, with either NADP+ or NAD+ as a cofactor in addition to shikimate, making this enzyme an important candidate for quinate production. Production of shikimate, quinate, 3-dehydroshikimate and other aromatic derivatives in strain PB12.SA22 during batch culture fermentation
synthesis
-
enzyme YdiB displays a clear activity on quinate, with either NADP+ or NAD+ as a cofactor in addition to shikimate, making this enzyme an important candidate for quinate production. Production of shikimate, quinate, 3-dehydroshikimate and other aromatic derivatives in strain PB12.SA22 during batch culture fermentation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.; Sauvé, 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-Å 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
Pinus sylvestris, Larix sibirica
-
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 faecalis, Enterococcus faecium, Lactiplantibacillus plantarum, Listeria monocytogenes, Salmonella enterica subsp. enterica serovar Typhimurium, Shigella flexneri, Streptococcus pyogenes, Escherichia coli (P0A6D5), Haemophilus influenzae (P44774)
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 (Q88GF6), Pseudomonas putida KT2440 (Q88JP1), Pseudomonas putida KT2440 (Q88K85)
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
Höppner, 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 (A4QB65), Corynebacterium glutamicum (Q9X5C9), 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
2016
Escherichia coli, Escherichia coli JM101
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.1.282)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
