Information on EC 1.1.5.8 - quinate dehydrogenase (quinone)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.5.8
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RECOMMENDED NAME
GeneOntology No.
quinate dehydrogenase (quinone)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
quinate + quinone = 3-dehydroquinate + quinol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
quinate degradation I
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shikimate degradation I
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quinate degradation
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Phenylalanine, tyrosine and tryptophan biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
115299-99-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain LMD 79.41
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Manually annotated by BRENDA team
strain SA1, SA4, SA5, SA6, SA7, SA8, SA9, SA10, SA11, SA12 and SA13, isolated in Thailand
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Manually annotated by BRENDA team
strain SA1, SA4, SA5, SA6, SA7, SA8, SA9, SA10, SA11, SA12 and SA13, isolated in Thailand
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Manually annotated by BRENDA team
strain IFO 3294
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Manually annotated by BRENDA team
gene qdh
UniProt
Manually annotated by BRENDA team
strain IFO 3244 and IFO 3292
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Manually annotated by BRENDA team
strain IFO 3244 and IFO 3292
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Manually annotated by BRENDA team
no activity in Gluconobacter albidus
IFO 3253
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Manually annotated by BRENDA team
no activity in Gluconobacter asaii
IFO 3265, IFO 3275 and IFO 3276
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Manually annotated by BRENDA team
no activity in Gluconobacter cerinus
IFO 3264, IFO 3268, IFo 3262 and IFO 3270
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Manually annotated by BRENDA team
no activity in Gluconobacter dioxyacetonicus
IFO 3271 and IFO 3272
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Manually annotated by BRENDA team
no activity in Gluconobacter frateurii
IFO 3251, IFO 3264, CHM 16, CHM 54 and IFO 3286
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Manually annotated by BRENDA team
no activity in Gluconobacter gluconicus
IFO 3285
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Manually annotated by BRENDA team
no activity in Gluconobacter industrius
IFO 3260-1, IFO 3260-2 and IFO 3261
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Manually annotated by BRENDA team
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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Manually annotated by BRENDA team
no activity in Gluconobacter sphaericus
IFO 12467
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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
D-quinate + tetramethyl-p-phenylenediamine
dehydroquinate + reduced tetramethyl-p-phenylenediamine
show the reaction diagram
quinate + 2,6-dichlorophenol indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
quinate + 2,6-dichlorophenol-indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol-indophenol
show the reaction diagram
quinate + ?
3-dehydroquinate + ?
show the reaction diagram
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dried cells or dried membrane frations incubated with quinate
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?
quinate + phenazine methosulfate
3-dehydroquinate + reduced phenazine methosulfate
show the reaction diagram
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
show the reaction diagram
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
show the reaction diagram
shikimate + 2,6-dichlorophenol indophenol
3-dehydroshikimate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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reaction rate is 74% of that with quinate
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?
additional information
?
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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
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyrroloquinoline quinone
pyrroloquinoline-quinone
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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divalent metal ion seems necessary
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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inhibits apoenzyme quinate dehydrogenase
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 hide
LITERATURE
IMAGE
0.89
2,6-dichlorophenol indophenol
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pH 6.5, 25C
0.52
potassium ferricyanide
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pH 6.5, 25C
0.2 - 1
quinate
0.26
shikimate
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pH 6.5, 25C, with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol as electron acceptor
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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5.8 micromol/g wet cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
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quinate oxidation with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
6
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with electron acceptor 2,6-dichlorophenolindophenol
7.5
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with electron acceptor Wurster's blue
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Show AA Sequence (368 entries)
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