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Information on EC 1.1.1.24 - quinate/shikimate dehydrogenase (NAD+)
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1.1.1.24 quinate/shikimate dehydrogenase (NAD+)IUBMB Comments
The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
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Word Map
- 1.1.1.24
- crassa
-
neurospora
- dehydratase
- dehydroquinate
- dehydroshikimate
- qa
- nidulans
- gluconobacter
-
quinoproteins
- calcoaceticus
- 3-dehydroquinase
- protocatechuate
- carrot
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
quinate dehydrogenase, quinate/shikimate dehydrogenase, cglqsdh, quinate 5-dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cgl0424
CglQSDH
dehydrogenase, quinate
-
-
-
-
QDH
quinate 5-dehydrogenase
-
-
ambiguous
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quinate dehydrogenase
quinate/shikimate dehydrogenase
quinate: oxidoreductase
-
-
-
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quinate:NAD oxidoreductase
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-
-
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quinate:NAD+ 5-oxidoreductase
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-
-
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quinic dehydrogenase
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-
ambiguous
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additional information
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the enzyme belongs to a functional class of the shikimate/quinate dehydrogenase family
quinate dehydrogenase
-
-
ambiguous
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quinate/shikimate dehydrogenase
the enzyme also shows activity with shikimate
quinate/shikimate dehydrogenase
the enzyme also shows activity with shikimate
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-quinate + NAD+ = 3-dehydroquinate + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-quinate:NAD+ 3-oxidoreductase
The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
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CAS REGISTRY NUMBER
COMMENTARY
9028-28-8
-
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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 + NADP+
3-dehydroquinate + NADPH + H+
low activity
-
-
r
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+
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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
-
-
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
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
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-
-
r
p-hydroxybenzoate + O2
protocatechuic acid + H2O
-
overview substrate specificity, some strains are using the substrate, some are not
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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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-
?
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 + NADH + 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 + NADH + 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
?
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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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?
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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-
?
additional information
?
-
product analysis by GC-MS
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-
-
additional information
?
-
product analysis by GC-MS
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-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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+
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
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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INHIBITOR
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
-
erythrose 4-phosphate plus phosphoenolpyruvate increase quinate oxidizing activity by 25%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics
-
1.4
3-dehydroquinate
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
0.164
L-quinate
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
0.0537
NAD+
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
0.102
NADH
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
281
3-dehydroquinate
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
298
NADH
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
127
L-quinate
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
139
NAD+
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
200.7
3-dehydroquinate
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
2921.6
NADH
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
774.4
L-quinate
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
2588.5
NAD+
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
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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