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Enzyme Nomenclature
Information on EC 1.1.1.24 - quinate dehydrogenase
for references in articles please use BRENDA:EC1.1.1.24
Word Map on EC 1.1.1.24
- 1.1.1.24
- shikimate
- crassa
-
neurospora
-
dehydratase
- qa
- nidulans
- dehydroshikimate
- gluconobacter
- dehydroquinate
-
quinoproteins
- 3-dehydroquinase
- calcoaceticus
- acinetobacter
- carrot
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.1.1.24
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RECOMMENDED NAME
GeneOntology No.
quinate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-quinate + NAD+ = 3-dehydroquinate + NADH + H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
oxidation
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-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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+.
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CAS REGISTRY NUMBER
COMMENTARY
9028-28-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; bifunctional enzyme: quinate (shikimate) dehydrogenase, different from EC 1.1.1.25
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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
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
QDH plays a key role in the quinate-degradation pathway
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-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Thr88 and Thr221 are involved in quinate binding
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-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
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-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme also shows activity with shikimate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent
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-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
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-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme also shows activity with shikimate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent
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-
r
p-hydroxybenzoate + O2
protocatechuic acid + H2O
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overview substrate specificity, some strains are using the substrate, some are not
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-
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p-hydroxybenzoate + O2
protocatechuic acid + H2O
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overview substrate specificity, some strains are using the substrate, some are not
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-
-
quinate + NAD+
5-dehydroquinate + NADH + H+
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first reaction in inducible quinic acid catabolic pathway
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-
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quinate + NAD+
5-dehydroquinate + NADH + H+
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overview substrate specificity, some strains are using the substrate, some are not
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-
?
shikimate + NAD+
3-dehydroshikimate + NADPH + H+
the enzyme also shows high activity with quinate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADPH + H+
the enzyme also shows high activity with quinate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent
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-
r
additional information
?
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addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
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-
-
additional information
?
-
-
the enzyme is involved in the quinate and shikimate metabolism, regulation, overview
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-
-
additional information
?
-
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the bifunctional enzyme shows quinate and shikimate dehydrogenase activities
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-
-
additional information
?
-
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the bifunctional enzyme shows quinate and shikimate dehydrogenase activities, interconversion of 5-dehydroquinate and 5-dehydroshikimate by dehydroquinase, EC 4.2.1.10, favouring 5-dehydroshikimate formation
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-
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additional information
?
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structure of the potential binding site of quinate and shikimate includign the the completely conserved residues Lys92 and Asp102, overview. The crystal structure reveals that in contrast to shikimate, quinate forms a hydrogen bond to the NAD+. In addition, the hydroxyl group of a conserved active-site threonine hydrogen binds to quinate more effectively than to shikimate. Also, the hydroxyl group of a conserved tyrosine approaches the carboxylate group of quinate more closely than it does the carboxylate group of shikimate, active site structure, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
QDH plays a key role in the quinate-degradation pathway
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Q9X5C9
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Q9X5C9
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
-
-
r
p-hydroxybenzoate + O2
protocatechuic acid + H2O
-
overview substrate specificity, some strains are using the substrate, some are not
-
-
-
p-hydroxybenzoate + O2
protocatechuic acid + H2O
-
overview substrate specificity, some strains are using the substrate, some are not
-
-
-
quinate + NAD+
5-dehydroquinate + NADH + H+
-
first reaction in inducible quinic acid catabolic pathway
-
-
-
additional information
?
-
-
addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
-
-
-
additional information
?
-
-
the enzyme is involved in the quinate and shikimate metabolism, regulation, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
erythrose 4-phosphate
-
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%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
quinic acid
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purification step Q1 HiTrapQ, cofactor NAD+; purification step Q2 HiTrapQ, cofactor NADP+
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
quinate dehydrogenase activity is highest early in fruit development abd declines in older fruit
additional information
-
quinate dehydrogenase activity is highest early in fruit development abd declines in older fruit
additional information
-
quinate dehydrogenase activity is highest early in fruit development and declines in older fruit
additional information
-
activity in infection-resistant hypocotyls remains constant, enzyme activity in hypocotyls susceptible to infection decreases about 50%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
quinate dehydrogenase activity is at a maximum around the time of greatest quinic acid accumulation in the early stages (less than 60 days after anthesis) of fruit development. It declines markedly in late fruit development
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; quinate dehydrogenase activity is at a maximum around the time of greatest quinic acid accumulation in the early stages (less than 60 days after anthesis) of fruit development. It declines markedly in late fruit development, and is higher in species that accumulate the largest amounts of quinic acid (Actinidia chinensis and Actinidia deliciosa)
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quinate dehydrogenase activity is at a maximum around the time of greatest quinic acid accumulation in the early stages (less than 60 days after anthesis) of fruit development. It declines markedly in late fruit development, and is higher in species that accumulate the largest amounts of quinic acid (Actinidia chinensis and Actinidia deliciosa)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025);
Q9X5C9
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025);
Q9X5C9
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025);
Q9X5C9
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025);
Q9X5C9
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
-
1 * 41000, SDS-PAGE in presence of urea or electrophoresis in presence of cetyltrimethyl ammonium bromide
additional information
-
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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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1 * 41000, SDS-PAGE in presence of urea or electrophoresis in presence of cetyltrimethyl ammonium bromide
additional information
-
seconfdary and tertiary enzyme structures, the enzyme is composed of two alphabetaalpha domains containing two discontinuous segments, Asp22-Asn127 and Gly287-Leu302, overview
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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 20°C. 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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
half-life of unprotected enzyme: 20 min, 180 min in presence of NaCl, completely stable in presence of quinate, shikimate or NADH
47
-
inactivation, kinetics vary in presence of quinate or shikimate, respectively
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme knockout results in loss of the ability to grow on quinate and/or shikimate
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.24)
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