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Literature summary extracted from

  • Adachi, O.; Yoshihara, N.; Tanasupawat, S.; Toyama, H.; Matsushita, K.
    Purification and characterization of membrane-bound quinoprotein quinate dehydrogenase (2003), Biosci. Biotechnol. Biochem., 67, 2115-2123.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.8 0.2
-
quinate pH 6.5, 25°C,with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol as electron acceptor Acinetobacter calcoaceticus
1.1.5.8 0.26
-
shikimate pH 6.5, 25°C, with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol as electron acceptor Acinetobacter calcoaceticus
1.1.5.8 0.52
-
potassium ferricyanide pH 6.5, 25°C Acinetobacter calcoaceticus
1.1.5.8 0.89
-
2,6-dichlorophenol indophenol pH 6.5, 25°C Acinetobacter calcoaceticus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.8 membrane
-
Acinetobacter calcoaceticus 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.5.8 88000
-
x * 88000, SDS-PAGE Acinetobacter calcoaceticus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.5.8 additional information Acinetobacter calcoaceticus 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 ?
-
?
1.1.5.8 additional information Acinetobacter calcoaceticus AC3 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 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.8 Acinetobacter calcoaceticus
-
AC3
-
1.1.5.8 Acinetobacter calcoaceticus AC3
-
AC3
-
1.1.5.8 Acinetobacter sp.
-
and strains SA4, SA5, SA6, SA7, SA8, SA9, SA10, SA11, SA12 and SA13, isolated in Thailand
-
1.1.5.8 Acinetobacter sp. SA1
-
and strains SA4, SA5, SA6, SA7, SA8, SA9, SA10, SA11, SA12 and SA13, isolated in Thailand
-
1.1.5.8 Gluconobacter oxydans
-
IFO 3292 and IFO 3244. No activity in IFP3990, IFO3189, IFO 3287, ATCC 621 and IFO 14819
-
1.1.5.8 Gluconobacter oxydans
-
IFO 3294
-
1.1.5.8 no activity in Gluconobacter albidus
-
IFO 3253
-
1.1.5.8 no activity in Gluconobacter asaii
-
IFO 3265, IFO 3275 and IFO 3276
-
1.1.5.8 no activity in Gluconobacter cerinus
-
IFO 3264, IFO 3268, IFo 3262 and IFO 3270
-
1.1.5.8 no activity in Gluconobacter dioxyacetonicus
-
IFO 3271 and IFO 3272
-
1.1.5.8 no activity in Gluconobacter frateurii
-
IFO 3251, IFO 3264, CHM 16, CHM 54 and IFO 3286
-
1.1.5.8 no activity in Gluconobacter gluconicus
-
IFO 3285
-
1.1.5.8 no activity in Gluconobacter industrius
-
IFO 3260-1, IFO 3260-2 and IFO 3261
-
1.1.5.8 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
-
1.1.5.8 no activity in Gluconobacter sphaericus
-
IFO 12467
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.8
-
Acinetobacter calcoaceticus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.5.8 21
-
-
Acinetobacter calcoaceticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.8 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 Acinetobacter calcoaceticus ?
-
?
1.1.5.8 additional information no oxidation of glucose, 3-dehydroquinate, 3-dehydroshikimate and myo-inositol Acinetobacter calcoaceticus ?
-
?
1.1.5.8 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 Acinetobacter calcoaceticus AC3 ?
-
?
1.1.5.8 additional information no oxidation of glucose, 3-dehydroquinate, 3-dehydroshikimate and myo-inositol Acinetobacter calcoaceticus AC3 ?
-
?
1.1.5.8 quinate + 2,6-dichlorophenol indophenol reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol Acinetobacter calcoaceticus 3-dehydroquinate + reduced 2,6-dichlorophenol indophenol
-
?
1.1.5.8 quinate + 2,6-dichlorophenol indophenol reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol Acinetobacter calcoaceticus AC3 3-dehydroquinate + reduced 2,6-dichlorophenol indophenol
-
?
1.1.5.8 quinate + phenazine methosulfate reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol Acinetobacter calcoaceticus 3-dehydroquinate + reduced phenazine methosulfate
-
?
1.1.5.8 quinate + phenazine methosulfate reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol Acinetobacter calcoaceticus AC3 3-dehydroquinate + reduced phenazine methosulfate
-
?
1.1.5.8 quinate + potassium ferricyanide
-
Acinetobacter calcoaceticus 3-dehydroquinate + reduced potassium ferricyanide
-
?
1.1.5.8 quinate + potassium ferricyanide
-
Acinetobacter sp. 3-dehydroquinate + reduced potassium ferricyanide
-
?
1.1.5.8 quinate + potassium ferricyanide
-
Gluconobacter oxydans 3-dehydroquinate + reduced potassium ferricyanide
-
?
1.1.5.8 quinate + potassium ferricyanide
-
Acinetobacter calcoaceticus AC3 3-dehydroquinate + reduced potassium ferricyanide
-
?
1.1.5.8 quinate + potassium ferricyanide
-
Acinetobacter sp. SA1 3-dehydroquinate + reduced potassium ferricyanide
-
?
1.1.5.8 shikimate + 2,6-dichlorophenol indophenol reaction rate is 74% of that with quinate, reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol Acinetobacter calcoaceticus 3-dehydroshikimate + reduced 2,6-dichlorophenol indophenol
-
?
1.1.5.8 shikimate + phenazine methosulfate reaction rate is 74% of that with quinate, reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol Acinetobacter calcoaceticus 3-dehydroshikimate + reduced phenazine methosulfate
-
?
1.1.5.8 shikimate + potassium ferricyanide reaction rate is 74% of that with quinate Acinetobacter calcoaceticus 3-dehydroshikimate + reduced potassium ferricyanide
-
?

Subunits

EC Number Subunits Comment Organism
1.1.5.8 ? x * 88000, SDS-PAGE Acinetobacter calcoaceticus
1.1.5.8 More on addition of pyrroloquinoline quinone the purified apoenzyme is conveted from a dimer to a monomer Acinetobacter calcoaceticus

Synonyms

EC Number Synonyms Comment Organism
1.1.5.8 NAD(P)-independent quinate dehydrogenase
-
Acinetobacter calcoaceticus
1.1.5.8 NAD(P)-independent quinate dehydrogenase
-
Acinetobacter sp.
1.1.5.8 NAD(P)-independent quinate dehydrogenase
-
Gluconobacter oxydans
1.1.5.8 QDH
-
Acinetobacter calcoaceticus
1.1.5.8 QDH
-
Acinetobacter sp.
1.1.5.8 QDH
-
Gluconobacter oxydans
1.1.5.8 quinate dehydrogenase
-
Acinetobacter calcoaceticus
1.1.5.8 quinate dehydrogenase
-
Acinetobacter sp.
1.1.5.8 quinate dehydrogenase
-
Gluconobacter oxydans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.5.8 5 6 quinate oxidation with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol Acinetobacter calcoaceticus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.8 pyrroloquinoline quinone
-
Acinetobacter calcoaceticus
1.1.5.8 pyrroloquinoline quinone
-
Acinetobacter sp.
1.1.5.8 pyrroloquinoline quinone
-
Gluconobacter oxydans