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Information on EC 1.1.5.8 - quinate/shikimate dehydrogenase (quinone)
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1.1.5.8 quinate/shikimate dehydrogenase (quinone)IUBMB Comments
The enzyme is membrane-bound. Does not use NAD(P)+ as acceptor. Contains pyrroloquinoline-quinone. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), 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
- 1.1.5.8
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quinoproteins
- gluconobacter
- oxydans
- calcoaceticus
- 3-dehydroquinate
- acinetobacter
- d-glucose
- 3-dehydroshikimate
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quinohemoprotein
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methylobacterium
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holo-forms
The enzyme appears in viruses and cellular organisms
Synonyms
pqq-dependent dehydrogenase, quinoprotein quinate dehydrogenase, nad(p)-independent quinate dehydrogenase, quinate dehydrogenase (quinone), 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, quinate (pyrroloquinoline-quinone)
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EC 1.1.99.25
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formerly
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NAD(P)+-independent quinate dehydrogenase
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NAD(P)-independent quinate dehydrogenase
PQQ-dependent dehydrogenase
PQQ-QDH
pyrroloquinoline quinone-dependent dehydrogenase
QDH
quiA
quinate dehydrogenase
quinate dehydrogenase (quinone)
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quinate:pyrroloquinoline-quinone 5-oxidoreductase
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quinoprotein quinate dehydrogenase
NAD(P)-independent quinate dehydrogenase
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pyrroloquinoline quinone-dependent dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
quinate + quinone = 3-dehydroquinate + quinol
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
quinate:quinol 3-oxidoreductase
The enzyme is membrane-bound. Does not use NAD(P)+ as acceptor. Contains pyrroloquinoline-quinone. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), 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
115299-99-5
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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
D-quinate + tetramethyl-p-phenylenediamine
3-dehydroquinate + reduced tetramethyl-p-phenylenediamine
quinate + 2,6-dichlorophenol indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol indophenol
quinate + 2,6-dichlorophenol-indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol-indophenol
quinate + ?
3-dehydroquinate + ?
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dried cells or dried membrane frations incubated with quinate
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?
shikimate + 2,6-dichlorophenol indophenol
3-dehydroshikimate + reduced 2,6-dichlorophenol indophenol
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reaction rate is 74% of that with quinate, reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
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?
shikimate + phenazine methosulfate
3-dehydroshikimate + reduced phenazine methosulfate
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reaction rate is 74% of that with quinate, reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
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?
shikimate + potassium ferricyanide
3-dehydroshikimate + reduced potassium ferricyanide
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reaction rate is 74% of that with quinate
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?
D-quinate + tetramethyl-p-phenylenediamine
3-dehydroquinate + reduced tetramethyl-p-phenylenediamine
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2,6-dichlorophenolindophenol can also act as electron acceptor
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?
D-quinate + tetramethyl-p-phenylenediamine
3-dehydroquinate + reduced tetramethyl-p-phenylenediamine
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2,6-dichlorophenolindophenol can also act as electron acceptor
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?
quinate + 2,6-dichlorophenol indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol indophenol
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reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
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?
quinate + 2,6-dichlorophenol indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol indophenol
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reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
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?
quinate + 2,6-dichlorophenol-indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol-indophenol
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?
quinate + 2,6-dichlorophenol-indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol-indophenol
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-
?
quinate + phenazine methosulfate
3-dehydroquinate + reduced phenazine methosulfate
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reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
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?
quinate + phenazine methosulfate
3-dehydroquinate + reduced phenazine methosulfate
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reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
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?
quinate + phenazine methosulfate
3-dehydroquinate + reduced phenazine methosulfate
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?
quinate + phenazine methosulfate
3-dehydroquinate + reduced phenazine methosulfate
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?
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
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?
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
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?
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
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?
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
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?
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
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?
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
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r
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
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r
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
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r
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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primary enzyme in quinate oxidation
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
QDH shows higher affinity to quinate than to shikimate
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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primary enzyme in quinate oxidation
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
QDH shows higher affinity to quinate than to shikimate
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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primary enzyme in quinate oxidation
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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primary enzyme in quinate oxidation
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?
additional information
?
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the enzyme is formed in presence or absence of quinate in the culture medium, although stronger induction is usually observed in the presence of quinate. The enzyme directly couples with the respiratory chain of the organisms, yielding bioenergy during substrate oxidation
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?
additional information
?
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no oxidation of glucose, 3-dehydroquinate, 3-dehydroshikimate and myo-inositol
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?
additional information
?
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the enzyme is formed in presence or absence of quinate in the culture medium, although stronger induction is usually observed in the presence of quinate. The enzyme directly couples with the respiratory chain of the organisms, yielding bioenergy during substrate oxidation
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?
additional information
?
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no oxidation of glucose, 3-dehydroquinate, 3-dehydroshikimate and myo-inositol
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?
additional information
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QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM
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?
additional information
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QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm
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additional information
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QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm
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additional information
?
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QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm
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additional information
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QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM
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?
additional information
?
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QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm
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additional information
?
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QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm
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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
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
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r
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
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r
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
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r
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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primary enzyme in quinate oxidation
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
QDH shows higher affinity to quinate than to shikimate
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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primary enzyme in quinate oxidation
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
QDH shows higher affinity to quinate than to shikimate
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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primary enzyme in quinate oxidation
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?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
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primary enzyme in quinate oxidation
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?
additional information
?
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the enzyme is formed in presence or absence of quinate in the culture medium, although stronger induction is usually observed in the presence of quinate. The enzyme directly couples with the respiratory chain of the organisms, yielding bioenergy during substrate oxidation
-
-
?
additional information
?
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-
the enzyme is formed in presence or absence of quinate in the culture medium, although stronger induction is usually observed in the presence of quinate. The enzyme directly couples with the respiratory chain of the organisms, yielding bioenergy during substrate oxidation
-
-
?
additional information
?
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QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM
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?
additional information
?
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QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
PQQ-dependent dehydrogenase
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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quinate dehydrogenase holoenzyme and quinate dehydrogenase apoenzyme after recombination with pyrroloquinoline quinone is not affected by EDTA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
shikimate
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pH 6.5, 25°C, with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol as electron acceptor
0.2
quinate
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pH 6.5, 25°C,with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol as electron acceptor
1
quinate
pH 8.0, temperature not specified in the publication, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
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quinate oxidation with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and strains SA4, SA5, SA6, SA7, SA8, SA9, SA10, SA11, SA12 and SA13, isolated in Thailand
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brenda
and strains SA4, SA5, SA6, SA7, SA8, SA9, SA10, SA11, SA12 and SA13, isolated in Thailand
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brenda
no activity in Gluconobacter frateurii
IFO 3251, IFO 3264, CHM 16, CHM 54 and IFO 3286
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brenda
no activity in Gluconobacter oxydans
IFO 3130, IFO 3172, IFO 3290, IFO 3289, IFO 12528, var. alphaIFO3254, car. alphaIFO 3255, var. alphaIFO 3256, var. alphaIFO 3257 and car. alphaIFO3258
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brenda
IFO 3292 and IFO 3244. No activity in IFP3990, IFO3189, IFO 3287, ATCC 621 and IFO 14819
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
evolution
phylogenetic distribution of QDH with in the membrane-bound, PQQ-dependent proteins of the publicly available Gluconobacter genomes, overview
evolution
phylogenetic distribution of QDH with in the membrane-bound, PQQ-dependent proteins of the publicly available Gluconobacter genomes, overview. The genetic sequence of the QDH of NBRC3292 is identical to that of NBRC3244, while the QDH of NBRC3293 is different in 7 amino acids from that of NBRC3244
evolution
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phylogenetic distribution of QDH with in the membrane-bound, PQQ-dependent proteins of the publicly available Gluconobacter genomes, overview
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evolution
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phylogenetic distribution of QDH with in the membrane-bound, PQQ-dependent proteins of the publicly available Gluconobacter genomes, overview. The genetic sequence of the QDH of NBRC3292 is identical to that of NBRC3244, while the QDH of NBRC3293 is different in 7 amino acids from that of NBRC3244
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physiological function
Gluconobacter oxydans produces 3-dehydroquinate by oxidation of quinate through a reaction catalyzed by the quinate dehydrogenase (QDH), membrane-bound, pyrroloquinoline quinone (PQQ)-dependent dehydrogenase
physiological function
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Gluconobacter oxydans produces 3-dehydroquinate by oxidation of quinate through a reaction catalyzed by the quinate dehydrogenase (QDH), membrane-bound, pyrroloquinoline quinone (PQQ)-dependent dehydrogenase
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physiological function
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Gluconobacter oxydans produces 3-dehydroquinate by oxidation of quinate through a reaction catalyzed by the quinate dehydrogenase (QDH), membrane-bound, pyrroloquinoline quinone (PQQ)-dependent dehydrogenase
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). QUIA_ACIAD
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
809
5
88196
Swiss-Prot
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QUIA_XANCJ
790
4
82897
Swiss-Prot
-
A0A484QZQ6_9ZZZZ
806
5
86148
TrEMBL
Secretory Pathway (Reliability: 1)
A0A484Q1A6_9ZZZZ
806
5
86166
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0L0M1U2_9BURK
241
4
25836
TrEMBL
-
A0A1Y0Y6E8_ACEPA
812
5
88264
TrEMBL
-
F0Q294_ACIAP
Acidovorax avenae (strain ATCC 19860 / DSM 7227 / CCUG 15838 / JCM 20985 / LMG 2117 / NCPPB 1011)
806
5
84887
TrEMBL
-