Information on EC 1.1.1.24 - quinate dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.24
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RECOMMENDED NAME
GeneOntology No.
quinate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-quinate + NAD+ = 3-dehydroquinate + NADH + H+
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Phenylalanine, tyrosine and tryptophan biosynthesis
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-
quinate degradation II
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SYSTEMATIC NAME
IUBMB Comments
L-quinate:NAD+ 3-oxidoreductase
The enzyme is specific for quinate as substrate; phenylpyruvate, phenylalanine, cinnamate and shikimate will not act as substrates. NAD+ cannot be replaced by NADP+.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-28-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
carrot
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Manually annotated by BRENDA team
bifunctional enzyme: quinate (shikimate) dehydrogenase
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Manually annotated by BRENDA team
infected with Fusarium sporotrichiella var. sporoides Bilai
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
diverse number of strains
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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 + NADH
quinate + NAD+
show the reaction diagram
L-quinate + NAD+
3-dehydroquinate + NADH + H+
show the reaction diagram
L-quinate + NAD+
5-dehydroquinate + NADH + H+
show the reaction diagram
-
-
-
-
r
p-hydroxybenzoate + O2
protocatechuic acid + H2O
show the reaction diagram
quinate + NAD+
5-dehydroquinate + NADH + H+
show the reaction diagram
quinic acid + NAD(P)+
dehydroquinic acid + NAD(P)H + H+
show the reaction diagram
shikimate + NAD+
3-dehydroshikimate + NADH + H+
show the reaction diagram
shikimate + NAD+
3-dehydroshikimate + NADPH + H+
show the reaction diagram
shikimate + NAD+
5-dehydroshikimate + NADH + H+
show the reaction diagram
-
-
-
-
r
shikimate + NAD+
?
show the reaction diagram
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 + NADH
quinate + NAD+
show the reaction diagram
L-quinate + NAD+
3-dehydroquinate + NADH + H+
show the reaction diagram
L-quinate + NAD+
5-dehydroquinate + NADH + H+
show the reaction diagram
-
-
-
-
r
p-hydroxybenzoate + O2
protocatechuic acid + H2O
show the reaction diagram
quinate + NAD+
5-dehydroquinate + NADH + H+
show the reaction diagram
quinic acid + NAD(P)+
dehydroquinic acid + NAD(P)H + H+
show the reaction diagram
shikimate + NAD+
3-dehydroshikimate + NADH + H+
show the reaction diagram
shikimate + NAD+
5-dehydroshikimate + NADH + H+
show the reaction diagram
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-
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r
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
-
no activity with NADP(H)
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no metal ion requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Hydroxybenzoic acid
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5-dehydroquinic acid
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Aromatic amino acids
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inhibit reduction of dehydroquinate
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chloromercuribenzene 4-sulfonate
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inhibits both activities of the enzyme
p-chloromercuribenzoate
shikimic acid
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competitive inhibition
Sulfhydryl inhibitors
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-
-
additional information
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the enzyme is strongly repressed by D-glucose
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Aromatic amino acids
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slightly increased quinate oxidation
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dithiothreitol
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erythrose 4-phosphate
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erythrose 4-phosphate plus phosphoenolpyruvate increase quinate oxidizing activity by 25%
phosphoenolpyruvate
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erythrose 4-phosphate plus phosphoenolpyruvate increase quinate oxidizing activity by 25%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047 - 0.45
3-dehydroquinate
1
Dehydroquinate
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1.6 - 10.2
L-quinate
0.031 - 0.87
NAD+
0.007 - 0.7
NADP+
0.005 - 0.12
NADPH
0.32 - 6.25
quinate
0.3 - 10.9
quinic acid
1.18 - 53.9
shikimate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50.8 - 104.9
L-quinate
43.7 - 223.1
NAD+
30.1 - 214.1
shikimate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33.3 - 44.05
L-quinate
2243
71.6 - 826.6
NAD+
7
3.1 - 4.2
shikimate
352
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3453
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3700 - 6500
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additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 9.5
substrate: L-quinate
9
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quinate dehydrogenase activity
10 - 10.5
substrate: shikimate
10
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shikimate dehydrogenase activity
additional information
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different pH optima for shikimate and quinate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9.8
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at pH 8.5 and 9.8 about 50% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
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gel filtration
35000
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gel filtration
40000
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1 * 40000 + 1 * 60000-63000, SDS-PAGE
41000
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1 * 41000, SDS-PAGE in presence of urea or electrophoresis in presence of cetyltrimethyl ammonium bromide
42000
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sucrose density gradient centrifugation
55000
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3 * 55000, SDS-PAGE
110000
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gel filtration
160000
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gel filtration
additional information
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transfer of carrot enzyme from dark to light conditions shifts MW from 42000 Da to 110000 Da, probably due to association of a regulatory subunit which may be a calciprotein
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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1 * 40000 + 1 * 60000-63000, SDS-PAGE
monomer
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1 * 41000, SDS-PAGE in presence of urea or electrophoresis in presence of cetyltrimethyl ammonium bromide
trimer
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3 * 55000, SDS-PAGE
additional information
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seconfdary and tertiary enzyme structures, the enzyme is composed of two alphabetaalpha domains containing two discontinuous segments, Asp22-Asn127 and Gly287-Leu302, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD+-dependent enzyme, X-ray diffraction structure determination and anaylsis at 1.64-8.0 A resolution, molecular replacement method, modelling of the ternary complexes, overview
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vapor diffusion sitting-drop method at 20C. Atomic resolution crystal structures of the enzyme in different functional states: with bound NAD+ (binary complex) and as ternary complexes with NADH plus either shikimate or quinate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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-20C, highest stability
286356
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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half-life of unprotected enzyme: 20 min, 180 min in presence of NaCl, completely stable in presence of quinate, shikimate or NADH
47
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inactivation, kinetics vary in presence of quinate or shikimate, respectively
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high ionic strength, such as 0.1 M (NH4)2SO4, NaCl or phosphate buffer or the presence of 0.1 M quinate or shikimate protects against thermal inactivation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, stable for several weeks, 30% loss of activity in 6 months
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-20C, 0.1 M NaCl, half-life 40 days
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-20C, pH 7.5, several weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme: quinate (shikimate) dehydrogenase
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partial from young kiwifruit by extraction and chromatography on Superdex G75 and HiTrapQ columns
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separation from NADP+-linked shikimate dehydrogenase, EC 1.1.1.25, gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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enzyme knockout results in loss of the ability to grow on quinate and/or shikimate