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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
-
quinoproteins
- gluconobacter
- oxydans
- calcoaceticus
- 3-dehydroquinate
- acinetobacter
- d-glucose
- 3-dehydroshikimate
-
quinohemoprotein
-
methylobacterium
-
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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-
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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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-
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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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-
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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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-
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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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-
-
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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
-
-
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
primary enzyme in quinate oxidation
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-
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
primary enzyme in quinate oxidation
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-
?
additional information
?
-
-
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
?
-
-
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
?
-
QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM
-
-
?
additional information
?
-
QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM
-
-
?
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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
-
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
-
-
brenda
and strains SA4, SA5, SA6, SA7, SA8, SA9, SA10, SA11, SA12 and SA13, isolated in Thailand
-
-
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
-
-
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
-
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
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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
-
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
-
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
-
Show AA Sequence and Transmembrane Helices (558 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 88600, about, sequence calculation, x * 100000, recombinant enzyme, SDS-PAGE
?
-
x * 88600, about, sequence calculation, x * 100000, recombinant enzyme, SDS-PAGE
-
additional information
-
on addition of pyrroloquinoline quinone the purified apoenzyme is conveted from a dimer to a monomer
additional information
-
on addition of pyrroloquinoline quinone the purified apoenzyme is conveted from a dimer to a monomer
-
additional information
prediction of secondary structure of the mRNA
additional information
prediction of secondary structure of the mRNA
additional information
-
prediction of secondary structure of the mRNA
-
additional information
-
prediction of secondary structure of the mRNA
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from cell membranes by dilution in 10 mM Tris-HCl, pH 7.5, 1 mM CaCl2, and 1% w/v DDM at the final protein concentration of 10 mg/ml followed by incubation for 30 min at 4°C with gentle mixing and ultracentrifugation at 100000 × g for 30 min at 4°C. The resultant supernatant containing the solubilized membranes is resuspended with the same volume of 10 mM Tris-HCl, pH 7.5, and 1 mM CaCl2. The enzyme is solublized from membranes and purified by anion exchange chromatography, dialysis, and hydroxyapatite chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene qdh, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression in pyrroloquinoline quinone synthesizing Pseudomonas putida strain HK5
gene quiA, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, heterologous expression of QDH in Gluconobacter frateurii, improvement of the heterologous expression of QDH in Gluconobacter strains using a broad-host-range plasmid, best with a long 5'-UTR. Gluconobacter oxydans strain NBRC12528 DELTAadhA::KmR is transformed by triparental mating using Escherichia coli HB101 harboring pRK2013 as the helper strain, Gluconobacter frateurii strain SEI46 (DELTAadhAB) is transformed with the same plasmids by electroporation
gene quiA, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, QDH translates from the second TTG codon: Met-His-Ser-Ile-Asp, heterologous expression of QDH in Gluconobacter frateurii, improvement of the heterologous expression of QDH in Gluconobacter strains using a broad-host-range plasmid, best with a long 5'-UTR. Gluconobacter oxydans strain NBRC12528 DELTAadhA::KmR is transformed by triparental mating using Escherichia coli HB101 harboring pRK2013 as the helper strain, Gluconobacter frateurii strain SEI46 (DELTAadhAB) is transformed with the same plasmids by electroporation. Change of the initiation codon to ATG does not improve QDH activity but results in expression levels similar to those achieved with the wild-type plasmid
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Van Kleef, M.A.G.; Duine, J.A.
Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein
Arch. Microbiol.
150
32-36
1988
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
brenda
Adachi, O.; Yoshihara, N.; Tanasupawat, S.; Toyama, H.; Matsushita, K.
Purification and characterization of membrane-bound quinoprotein quinate dehydrogenase
Biosci. Biotechnol. Biochem.
67
2115-2123
2003
Gluconobacter oxydans, Acinetobacter calcoaceticus, Acinetobacter sp., no activity in Gluconobacter gluconicus, no activity in Gluconobacter industrius, no activity in Gluconobacter sphaericus, no activity in Gluconobacter oxydans, no activity in Gluconobacter asaii, no activity in Gluconobacter albidus, no activity in Gluconobacter cerinus, no activity in Gluconobacter dioxyacetonicus, no activity in Gluconobacter frateurii, Acinetobacter calcoaceticus AC3, Acinetobacter sp. SA1
brenda
Adachi, O.; Tanasupawat, S.; Yoshihara, N.; Toyama, H.; Matsushita, K.
3-Dehydroquinate production by oxidative fermentation and further conversion of 3-dehydroquinate to the intermediates in the shikimate pathway
Biosci. Biotechnol. Biochem.
67
2124-2131
2003
Gluconobacter oxydans, Gluconobacter sp., Gluconobacter oxydans IFO 3294, Gluconobacter sp. IFO 3244
brenda
Adachi, O.; Ano, Y.; Toyama, H.; Matsushita, K.
High shikimate production from quinate with two enzymatic systems of acetic acid bacteria
Biosci. Biotechnol. Biochem.
70
2579-2582
2006
Gluconobacter oxydans
brenda
Vangnai, A.S.; Promden, W.; De-Eknamkul, W.; Matsushita, K.; Toyama, H.
Molecular characterization and heterologous expression of quinate dehydrogenase gene from Gluconobacter oxydans IFO3244
Biochemistry (Moscow)
75
452-459
2010
Gluconobacter oxydans (B9TTF1), Gluconobacter oxydans IFO3244 (B9TTF1)
brenda
Yakushi, T.; Komatsu, K.; Matsutani, M.; Kataoka, N.; Vangnai, A.S.; Toyama, H.; Adachi, O.; Matsushita, K.
Improved heterologous expression of the membrane-bound quinoprotein quinate dehydrogenase from Gluconobacter oxydans
Protein Expr. Purif.
145
100-107
2018
Gluconobacter oxydans (A0A2Z5U248), Gluconobacter oxydans (A0A2Z5U421), Gluconobacter oxydans, Gluconobacter oxydans NBRC32