Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-dehydroquinate + NADPH + H+
L-quinate + NADP+
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway
-
-
?
3-dehydroshikimate + NADH + H+
shikimate + NAD+
-
-
-
r
dihydroshikimate + NAD+
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
L-quinate + 3-acetylpyridine adenine dinucleotide
3-dehydroquinate + ?
L-quinate + beta-NAD+
3-dehydroquinate + beta-NADH + H+
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
L-quinate + NAD+
3-dehydroquinate + NADH + H+
L-quinate + NADP+
3-dehydroquinate + NADPH + 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+
-
-
-
?
quinate + NAD+
3-dehydroquinate + NADH + H+
quinate + NADP+
3-dehydroquinate + NADPH + H+
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD+
3-dehydroshikimate + NADH + H+
shikimate + NADP+
3-dehydroshikimate + NADPH + 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
-
-
?
additional information
?
-
3-dehydroquinate + NADPH + H+
L-quinate + NADP+
-
-
-
r
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+
-
-
-
-
?
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+
-
-
-
-
?
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
-
-
-
-
?
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(P)+
3-dehydroquinate + NAD(P)H + H+
-
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold greater with quinate than with shikimate
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
0.3% of the activity with NAD+
-
-
?
quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
?
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+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + 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+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, a single enzyme with both quinate and shikimate dehydrogenase activity, 72% of the activity with (-)-quinate
(-)-enantiomer, reverse reaction: 15% of the activity with (-)-3-dehydroquinate
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold lower with shikimate than with quinate
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
very low activity with NADP+
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
very low activity with NADP+
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
additional information
?
-
the enzyme CglQSDH shows a substrate preference for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes
-
-
?
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
?
-
-
role in quinic acid metabolism
-
-
?
additional information
?
-
-
catalyzes the first reaction in the inducible quinic acid catabolic pathway
-
-
?
additional information
?
-
-
NAD+-utilizing QDHs are more active with quinate than with shikimate
-
-
-
additional information
?
-
-
role in quinic acid metabolism
-
-
?
additional information
?
-
-
enzyme PintaQDH reacts equally well with both shikimate and quinate
-
-
-
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
-
-
?
additional information
?
-
NAD+-utilizing QDHs are more active with quinate than with shikimate
-
-
-
additional information
?
-
NAD+-utilizing QDHs are more active with quinate than with shikimate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + NAD+
3-dehydroquinate + NADH + H+
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
quinate + NAD+
3-dehydroquinate + NADH + H+
quinate + NADP+
3-dehydroquinate + NADPH + H+
shikimate + NAD+
3-dehydroshikimate + NADH + H+
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
additional information
?
-
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
?
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
?
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + 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+
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
?
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+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
additional information
?
-
the enzyme CglQSDH shows a substrate preference for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes
-
-
?
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
?
-
-
role in quinic acid metabolism
-
-
?
additional information
?
-
-
catalyzes the first reaction in the inducible quinic acid catabolic pathway
-
-
?
additional information
?
-
-
role in quinic acid metabolism
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.65
3-acetylpyridine adenine dinucleotide
-
pH 10, cosubstrate (-)-quinate
0.42 - 1.141
3-dehydroquinate
0.2 - 5.933
3-dehydroshikimate
0.15
beta-NAD+
-
pH 10, cosubstrate (-)-quinate
2.56
dihydroshikimate
-
pH 10, (-)-enantiomer, cosubstrate NAD+
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+
additional information
additional information
-
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
0.2
3-dehydroshikimate
with NADPH, pH 7.0, 30°C
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
0.0054
L-quinate
mutant Y39F, 20°C, pH 9.0
0.0057
L-quinate
mutant S22A, 20°C, pH 9.0
0.0091
L-quinate
wild type enzyme, 20°C, pH 9.0
0.0136
L-quinate
mutant Q262A, 20°C, pH 9.0
0.0157
L-quinate
mutant S67A, 20°C, pH 9.0
0.041
L-quinate
pH 9, 20°C, cosubstrate NAD+
0.321
L-quinate
-
with NAD+, isozyme Poptr3, pH 8.5, 22°C
0.334
L-quinate
-
with NAD+, isozyme Poptr2, pH 8.5, 22°C
0.444
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
0.555
L-quinate
pH 9, 20°C, cosubstrate NADP+
0.677
L-quinate
-
pH and temperature not specified in the publication, enzyme PintaQDH with NADP+
1.56
L-quinate
pH 7.5, 30°C, with NAD+
1.88
L-quinate
pH 8.8, 25°C, with NAD+
2.38
L-quinate
pH 9.0-9.5, 30°C, with NAD+
2.541
L-quinate
with NADPH, pH 7.0, 30°C
2.95
L-quinate
-
pH 10, (-)-enantiomer, cosubstrate NAD+
3.4 - 3.6
L-quinate
-
pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase
20.52
L-quinate
mutant T106A, 20°C, pH 9.0
32.68
L-quinate
mutant K71A, 20°C, pH 9.0
0.0004
NAD+
mutant K71A, in the presence of shikimate, 20°C, pH 9.0
0.002
NAD+
mutant K71A, in the presence of L-quinate, 20°C, pH 9.0
0.0068
NAD+
mutant D107A, in the presence of shikimate, 20°C, pH 9.0
0.0107
NAD+
mutant Q262A, in the presence of shikimate, 20°C, pH 9.0
0.0121
NAD+
mutant S67A, in the presence of L-quinate, 20°C, pH 9.0
0.0122
NAD+
wild type enzyme, in the presence of shikimate, 20°C, pH 9.0
0.0125
NAD+
mutant Y39F, in the presence of L-quinate, 20°C, pH 9.0
0.0126
NAD+
mutant S67A, in the presence of shikimate, 20°C, pH 9.0
0.0142
NAD+
mutant Q262A, in the presence of L-quinate, 20°C, pH 9.0
0.0158
NAD+
mutant T106A, in the presence of shihikimat, 20°C, pH 9.0
0.0158
NAD+
mutant Y39F, in the presence of shikimate, 20°C, pH 9.0
0.0168
NAD+
mutant S22A, in the presence of L-quinate, 20°C, pH 9.0
0.018
NAD+
mutant S22A, in the presence of shikimate, 20°C, pH 9.0
0.018
NAD+
with shikimate, pH 8.6, 30°C
0.0184
NAD+
wild type enzyme, in the presence of L-quinate, 20°C, pH 9.0
0.0578
NAD+
mutant T106A, in the presence of L-quinate, 20°C, pH 9.0
0.087
NAD+
pH 9, 20°C, cosubstrate shikimate
0.116
NAD+
pH 9, 20°C, cosubstrate L-quinate
0.13
NAD+
pH 7.5, 30°C, with quinate
0.28
NAD+
pH 9.0-9.5, 30°C, with quinate
0.314
NAD+
-
with shikimate, pH and temperature not specified in the publication
0.43
NAD+
pH 8.8, 25°C, with quinate
0.46
NAD+
pH 10.0-10.5, 30°C, with shikimate
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
0.572
NAD+
in the presence of shikimate
0.635
NAD+
with quinate, pH and temperature not specified in the publication
0.71
NAD+
pH 8.8, 25°C, with shikimate
0.87
NAD+
pH 7.5, 30°C, with shikimate
1.083
NAD+
in the presence of quinate
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
0.1
NADP+
pH 9, 20°C, cosubstrate shikimate
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
0.5
NADP+
pH 9, 20°C, cosubstrate L-quinate
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
2.65
NADP+
pH 8.8, 25°C, with shikimate
0.107
quinate
-
with NAD+, pH and temperature not specified in the publication
0.129
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
0.783
quinate
in the presence of 2 mM NAD+
0.0017
shikimate
mutant S67A, 20°C, pH 9.0
0.0028
shikimate
mutant Q262A, 20°C, pH 9.0
0.0029
shikimate
wild type enzyme, 20°C, pH 9.0
0.0032
shikimate
mutant S22A, 20°C, pH 9.0
0.0032
shikimate
mutant Y39F, 20°C, pH 9.0
0.02
shikimate
pH 9, 20°C, cosubstrate NAD+
0.12
shikimate
pH 9, 20°C, cosubstrate NADP+
0.187
shikimate
with NADP+, pH 7.0, 30°C
0.199
shikimate
mutant T106A, 20°C, pH 9.0
0.26
shikimate
with NAD+, pH 8.6, 30°C
0.392
shikimate
-
with NAD+, isozyme Poptr3, pH 8.5, 22°C
0.513
shikimate
mutant K71A, 20°C, pH 9.0
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+
0.833
shikimate
-
with NAD+, isozyme Poptr2, pH 8.5, 22°C
1.299
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
2.18
shikimate
pH 8.8, 25°C, with NADP+
3.38
shikimate
pH 8.8, 25°C, with NAD+
4.2
shikimate
in the presence of 2 mM NAD+
5.25
shikimate
-
pH 10, (-)-enantiomer, cosubstrate NAD+
10.16
shikimate
pH 7.5, 30°C, with NAD+
40.07
shikimate
mutant D107A, 20°C, pH 9.0
55.88
shikimate
pH 10.0-10.5, 30°C, with NAD+
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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.
9.31 - 114
3-dehydroquinate
5.67 - 329
3-dehydroshikimate
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
329
3-dehydroshikimate
with NADPH, pH 7.0, 30°C
0.0063
L-quinate
pH 8.8, 25°C, with NAD+
0.012
L-quinate
mutant K71A, 20°C, pH 9.0
0.024
L-quinate
mutant S67A, 20°C, pH 9.0
0.036
L-quinate
with NADPH, pH 7.0, 30°C
0.05
L-quinate
pH 9, 20°C, cosubstrate NAD+ or NADP+
0.05
L-quinate
mutant Q262A, 20°C, pH 9.0
0.06
L-quinate
mutant Y39F, 20°C, pH 9.0
0.068
L-quinate
mutant S22A, 20°C, pH 9.0
0.113
L-quinate
wild type enzyme, 20°C, pH 9.0
0.233
L-quinate
mutant T106A, 20°C, pH 9.0
14.6
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
50.82
L-quinate
pH 7.5, 30°C, with NAD+
104.9
L-quinate
pH 9.0-9.5, 30°C, with NAD+
0.004
NAD+
mutant K71A, in the presence of L-quinate, 20°C, pH 9.0
0.0055
NAD+
pH 8.8, 25°C, with quinate
0.012
NAD+
mutant K71A, in the presence of shikimate, 20°C, pH 9.0
0.022
NAD+
mutant D107A, in the presence of shikimate, 20°C, pH 9.0
0.022
NAD+
mutant Q262A, in the presence of shikimate, 20°C, pH 9.0
0.023
NAD+
mutant S67A, in the presence of L-quinate, 20°C, pH 9.0
0.043
NAD+
mutant Q262A, in the presence of L-quinate, 20°C, pH 9.0
0.05
NAD+
pH 9, 20°C, cosubstrate shikimate or L-quinate
0.082
NAD+
mutant S22A, in the presence of L-quinate, 20°C, pH 9.0
0.09
NAD+
mutant Y39F, in the presence of L-quinate, 20°C, pH 9.0
0.105
NAD+
wild type enzyme, in the presence of shikimate, 20°C, pH 9.0
0.108
NAD+
mutant T106A, in the presence of shihikimat, 20°C, pH 9.0
0.122
NAD+
mutant T106A, in the presence of L-quinate, 20°C, pH 9.0
0.142
NAD+
wild type enzyme, in the presence of L-quinate, 20°C, pH 9.0
0.153
NAD+
mutant S22A, in the presence of shikimate, 20°C, pH 9.0
0.178
NAD+
mutant S67A, in the presence of shikimate, 20°C, pH 9.0
0.24
NAD+
mutant Y39F, in the presence of shikimate, 20°C, pH 9.0
0.74
NAD+
with shikimate, pH and temperature not specified in the publication
2.8
NAD+
pH 8.8, 25°C, with shikimate
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
43.67
NAD+
pH 7.5, 30°C, with quinate
55.7
NAD+
in the presence of quinate
61.1
NAD+
in the presence of shikimate
61.12
NAD+
pH 7.5, 30°C, with shikimate
105.8
NAD+
pH 10.0-10.5, 30°C, with shikimate
223.1
NAD+
pH 9.0-9.5, 30°C, with quinate
0.0018
NADP+
-
with quinate, pH and temperature not specified in the publication
0.022
NADP+
pH 8.8, 25°C, with shikimate
0.05
NADP+
pH 9, 20°C, cosubstrate L-quinate
0.117
NADP+
pH 9, 20°C, cosubstrate shikimate
0.335
NADP+
-
with shikimate, pH and temperature not specified in the publication
7
NADP+
-
with quinate, pH and temperature not specified in the publication
8.6
NADP+
-
with shikimate, pH and temperature not specified in the publication
0.493
quinate
-
with NAD+, pH and temperature not specified in the publication
8.5
quinate
-
with NAD+, 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
37.7
quinate
in the presence of 2 mM NAD+
0.011
shikimate
mutant K71A, 20°C, pH 9.0
0.027
shikimate
pH 8.8, 25°C, with NADP+
0.05
shikimate
pH 9, 20°C, cosubstrate NAD+
0.05
shikimate
mutant Q262A, 20°C, pH 9.0
0.054
shikimate
mutant T106A, 20°C, pH 9.0
0.091
shikimate
wild type enzyme, 20°C, pH 9.0
0.109
shikimate
mutant S22A, 20°C, pH 9.0
0.117
shikimate
pH 9, 20°C, cosubstrate NADP+
0.132
shikimate
mutant D107A, 20°C, pH 9.0
0.148
shikimate
mutant S67A, 20°C, pH 9.0
0.187
shikimate
mutant Y39F, 20°C, pH 9.0
1.75
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
3.9
shikimate
pH 8.8, 25°C, with NAD+
9.6
shikimate
with NAD+, pH 8.6, 30°C
30.13
shikimate
pH 7.5, 30°C, with NAD+
31.1
shikimate
with NADP+, pH 7.0, 30°C
55.7
shikimate
in the presence of 2 mM NAD+
214.1
shikimate
pH 10.0-10.5, 30°C, with NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
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
-
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
-
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
-
reactions comprising the shikimate/quinate cycle, overview
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
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
-
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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 (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
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
Brassica napus, Brassica rapa, Nicotiana tabacum, Solanum lycopersicum (A0A3Q7H2B2), Solanum lycopersicum (A0A3Q7IET9)
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