Information on EC 1.1.1.282 - quinate/shikimate dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.282
-
RECOMMENDED NAME
GeneOntology No.
quinate/shikimate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
show the reaction diagram
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
chorismate biosynthesis from 3-dehydroquinate
-
-
Metabolic pathways
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
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chorismate metabolism
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-87-3
cf. EC 1.1.1.25
9028-28-8
cf. EC 1.1.1.24
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
12 years old
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
20 days old saplings
-
-
Manually annotated by BRENDA team
20 years old
-
-
Manually annotated by BRENDA team
strain N75
-
-
Manually annotated by BRENDA team
strain N75
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-dehydroquinate + NADPH + H+
L-quinate + NADP+
show the reaction diagram
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
show the reaction diagram
-
YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway
-
-
?
3-dehydroshikimate + NADH + H+
shikimate + NAD+
show the reaction diagram
-
-
-
-
r
dihydroshikimate + NAD+
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
show the reaction diagram
L-quinate + 3-acetylpyridine adenine dinucleotide
3-dehydroquinate + ?
show the reaction diagram
L-quinate + beta-NAD+
3-dehydroquinate + beta-NADH + H+
show the reaction diagram
L-quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
show the reaction diagram
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
show the reaction diagram
L-quinate + nicotinamide 1,N6-ethenoadenine dinucleotide
3-dehydroquinate + ?
show the reaction diagram
-
69% of the activity with NAD+
-
-
?
L-quinate + nicotinamide hypoxanthine dinucleotide
3-dehydroquinate + ?
show the reaction diagram
-
1.3fold higher activity than with NAD+
-
-
?
quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
show the reaction diagram
-
-
-
?
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
show the reaction diagram
shikimate + NAD+
3-dehydroshikimate + NADH + H+
show the reaction diagram
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
show the reaction diagram
-
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
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate + NAD+
4-hydroxy-3-oxocyclohexane-c-1-carboxylate + NADH + H+
show the reaction diagram
-
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+
?
show the reaction diagram
-
6% of the activity with (-)-quinate
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-dehydroquinate + NADPH + H+
L-quinate + NADP+
show the reaction diagram
-
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)+
show the reaction diagram
-
YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
-
67% of the activity with NAD+
NADP+
NADPH
nicotinamide 1,N6-ethenoadenine dinucleotide
-
69% of the activity with NAD+
nicotinamide hypoxanthine dinucleotide
-
1.3fold higher activity than with NAD+
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
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-quinate
-
competitive inhibitor with respect to shikimate
shikimate
-
competitive inhibitor with respect to L-quinate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65
3-acetylpyridine adenine dinucleotide
-
pH 10, cosubstrate (-)-quinate
0.15
beta-NAD+
-
pH 10, cosubstrate (-)-quinate
1 - 5.3
Dehydroquinate
2.56
dihydroshikimate
-
pH 10, (-)-enantiomer, cosubstrate NAD+
0.0054 - 32.68
L-quinate
0.0004 - 1.083
NAD+
0.001 - 0.5
NADP+
0.005 - 0.012
NADPH
-
pH 10, 20°C, cosubstrate dehydroquinate, both forms of quinate (shikimate) dehydrogenase
0.51
nicotinamide 1,N6-ethanoadenine dinucleotide
-
pH 10, cosubstrate (-)-quinate
0.48
nicotinamide hypoxanthine dinucleotide
-
pH 10, cosubstrate (-)-quinate
0.783
quinate
in the presence of 2 mM NAD+
0.0017 - 40.07
shikimate
2.47
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate
-
pH 10, (-)-enantiomer, cosubstrate NAD+
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 0.233
L-quinate
0.004 - 61.1
NAD+
0.05 - 0.117
NADP+
37.7
quinate
Pseudomonas putida KT2440
Q88GF6, Q88JP1, Q88K85
in the presence of 2 mM NAD+
0.011 - 55.7
shikimate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00383
-
needles of 20 days old saplings, quinate and NADP+ as substrates
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
reduction reaction, assay at
7.7
-
back reaction, dehydroquinate or dehydroshikimate and NADPH as substrates
9
-
assay at
10
-
oxidation reaction, quinate or shikimate as substrates, 50 mM glycine-KOH
10.3
-
quinate or shikimate and NADP+ as substrates
10.6
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
of 20 days old saplings
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31350
-
2 * 31350, wild type enzyme, gel filtration
31500
-
1 * 31500, SDS-PAGE
33000
-
SDS-PAGE, mutant N92A
35000
-
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration
41000
-
1 * 41000
44000
-
gel filtration
53000
-
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration
57000
-
SDS-PAGE, wild type enzyme
64000
-
apoprotein, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
-
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
YdiB, with bound cofactors NAD+ or NADP+
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
t1/2: 1.85 min
additional information
-
the thermal stability of enzyme is greatly enhanced by low concentrations of quinate, shikimate, NADH or high ionic strength
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3000fold, two forms of the bifunctional quinate (shikimate) dehydrogenase: P1 and P2
-
by nickel-nitrilotriacetic acid affinity chromatography; by nickel-nitrilotriacetic acid affinity chromatography; by nickel-nitrilotriacetic acid affinity chromatography
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); 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); 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)
ydiB gene, expression in Escherichia coli BL21(DE3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D107A
-
site-directed mutagenesis
K71G
-
site-directed mutagenesis
N92A
-
site-directed mutagenesis
Q262A
-
site-directed mutagenesis
S22A
-
site-directed mutagenesis
S67A
-
site-directed mutagenesis, increased activity compared to wild type enzyme
T106A
-
site-directed mutagenesis
Y39F
-
site-directed mutagenesis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
development of novel herbicides
medicine
-
development of novel antimicrobial agents
pharmacology
-
enzymes of the shikimate pathway has been promoted as a target for the development of antimicrobial agents
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