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Information on EC 1.1.5.7 - cyclic alcohol dehydrogenase (quinone)
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1.1.5.7 cyclic alcohol dehydrogenase (quinone)IUBMB Comments
This enzyme oxidizes a wide variety of cyclic alcohols. Some minor enzyme activity is found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols. The enzyme is unable to catalyse the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols. This enzyme differs from EC 1.1.5.5, alcohol dehydrogenase (quinone), which shows activity with ethanol .
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The expected taxonomic range for this enzyme is: Gluconobacter frateurii
Synonyms
MCAD, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MCAD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a cyclic alcohol + a quinone = a cyclic ketone + a quinol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
cyclic alcohol:quinone oxidoreductase
This enzyme oxidizes a wide variety of cyclic alcohols. Some minor enzyme activity is found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols. The enzyme is unable to catalyse the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols. This enzyme differs from EC 1.1.5.5, alcohol dehydrogenase (quinone), which shows activity with ethanol [1].
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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
(2R,3R)-2,3-butanediol + pyrroloquinoline quinone
?
-
41% of the activity compared to cyclopentanol
-
-
ir
1,2-butanediol + pyrroloquinoline quinone
?
-
63% of the activity compared to cyclopentanol
-
-
ir
1,3-butanediol + pyrroloquinoline quinone
?
-
12% of the activity compared to cyclopentanol
-
-
ir
1,3-cyclopentanediol + pyrroloquinoline quinone
?
-
73% of the activity compared to cyclopentanol
-
-
ir
1,4-cyclohexanediol + pyrroloquinoline quinone
?
-
14% of the activity compared to cyclopentanol
-
-
ir
2,3-butanediol + pyrroloquinoline quinone
?
-
186% of the activity compared to cyclopentanol
-
-
ir
2,4-pentanediol + pyrroloquinoline quinone
?
-
16% of the activity compared to cyclopentanol
-
-
ir
2-hexanol + pyrroloquinoline quinone
2-hexanone + pyrroloquinoline quinol
-
10% of the activity compared to cyclopentanol
-
-
ir
2-methyl-2,4-pentanediol + pyrroloquinoline quinone
?
-
17% of the activity compared to cyclopentanol
-
-
ir
2-propanol + pyrroloquinoline quinone
acetone + pyrroloquinoline quinol
-
17% of the activity compared to cyclopentanol
-
-
ir
3-pentanol + pyrroloquinoline quinone
3-pentanone + pyrroloquinoline quinol
-
74% of the activity compared to cyclopentanol
-
-
ir
cis-1,2-cyclohexanediol + pyrroloquinoline quinone
?
-
88% of the activity compared to cyclopentanol
-
-
ir
cis-1,2-cyclopentanediol + pyrroloquinoline quinone
?
-
181% of the activity compared to cyclopentanol
-
-
ir
cis-4-cyclopentene-1,3-diol + pyrroloquinoline quinone
?
-
32% of the activity compared to cyclopentanol
-
-
ir
cyclobutanol + pyrroloquinoline quinone
cyclobutanone + pyrroloquinoline quinol
-
73% of the activity compared to cyclopentanol
-
-
ir
cyclohexanol + pyrroloquinoline quinone
cyclohexanone + pyrroloquinoline quinol
-
73% of the activity compared to cyclopentanol
-
-
ir
cyclooctanol + pyrroloquinoline quinone
cyclooctanone + pyrroloquinoline quinol
-
137% of the activity compared to cyclopentanol
-
-
ir
cyclopentanol + pyrroloquinoline quinone
cyclopentanone + pyrroloquinoline quinol
-
only pyrroloquinoline quinone is effective as electron acceptor, no activity with FAD, FMN and NAD(P)+
-
-
ir
D-arabitol + pyrroloquinoline quinone
?
-
78% of the activity compared to cyclopentanol
-
-
ir
D-mannitol + pyrroloquinoline quinone
?
-
25% of the activity compared to cyclopentanol
-
-
ir
D-sorbitol + pyrroloquinoline quinone
?
-
34% of the activity compared to cyclopentanol
-
-
ir
glycerol + pyrroloquinoline quinone
?
-
59% of the activity compared to cyclopentanol
-
-
ir
meso-erythritol + pyrroloquinoline quinone
?
-
100% of the activity compared to cyclopentanol
-
-
ir
ribitol + pyrroloquinoline quinone
?
-
34% of the activity compared to cyclopentanol
-
-
ir
(1R,2R)-trans-1,2-cyclohexanediol + pyrroloquinoline quinone
?
-
74% of the activity compared to cyclopentanol
-
-
ir
(1R,2R)-trans-1,2-cyclohexanediol + pyrroloquinoline quinone
?
-
74% of the activity compared to cyclopentanol
-
-
ir
(1S,2S)-trans-1,2-cyclohexanediol + pyrroloquinoline quinone
?
-
11% of the activity compared to cyclopentanol
-
-
ir
(1S,2S)-trans-1,2-cyclohexanediol + pyrroloquinoline quinone
?
-
11% of the activity compared to cyclopentanol
-
-
ir
2-butanol + pyrroloquinoline quinone
butane-2-one + reduced pyrroloquinoline quinone
-
41% of the activity compared to cyclopentanol
-
-
ir
2-butanol + pyrroloquinoline quinone
butane-2-one + reduced pyrroloquinoline quinone
-
41% of the activity compared to cyclopentanol
-
-
ir
additional information
?
-
-
the localization of the enzyme on the outer surface of the organism is advantageous to facilitate the oxidative fermentation of the cyclic alcohols. Since cyclic alcohols have some biological toxicity to living cells, according to the mechanism of the oxidative fermentation, there is no need to incorporate such toxic compounds into the cytoplasm to oxidize and pump out the oxidation products across the cytoplasmic membrane by the expense of bioenergy. The enzyme not inducible
-
-
?
additional information
?
-
-
the enzyme is unable to catalyze the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols. This enzyme oxidizes a wide variety of cyclic alcohols. Some minor enzyme activity is found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols
-
-
?
additional information
?
-
-
the localization of the enzyme on the outer surface of the organism is advantageous to facilitate the oxidative fermentation of the cyclic alcohols. Since cyclic alcohols have some biological toxicity to living cells, according to the mechanism of the oxidative fermentation, there is no need to incorporate such toxic compounds into the cytoplasm to oxidize and pump out the oxidation products across the cytoplasmic membrane by the expense of bioenergy. The enzyme not inducible
-
-
?
additional information
?
-
-
the enzyme is unable to catalyze the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols. This enzyme oxidizes a wide variety of cyclic alcohols. Some minor enzyme activity is found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols
-
-
?
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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
additional information
?
-
-
the localization of the enzyme on the outer surface of the organism is advantageous to facilitate the oxidative fermentation of the cyclic alcohols. Since cyclic alcohols have some biological toxicity to living cells, according to the mechanism of the oxidative fermentation, there is no need to incorporate such toxic compounds into the cytoplasm to oxidize and pump out the oxidation products across the cytoplasmic membrane by the expense of bioenergy. The enzyme not inducible
-
-
?
additional information
?
-
-
the localization of the enzyme on the outer surface of the organism is advantageous to facilitate the oxidative fermentation of the cyclic alcohols. Since cyclic alcohols have some biological toxicity to living cells, according to the mechanism of the oxidative fermentation, there is no need to incorporate such toxic compounds into the cytoplasm to oxidize and pump out the oxidation products across the cytoplasmic membrane by the expense of bioenergy. The enzyme not inducible
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
only pyrroloquinoline quinone is effective as electron acceptor, no activity with FAD, FMN and NAD(P)+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
addition of pyrroloquinoline quinone and Ca2+ converts the apo-enzyme to the holoenzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
localization of the enzyme on the outer surface of the organism is advantageous to facilitate the oxidative fermentation of the cyclic alcohols. Since cyclic alcohols have some biological toxicity to living cells, according to the mechanism of the oxidative fermentation, there is no need to incorporate such toxic compounds into the cytoplasm
brenda
-
localization of the enzyme on the outer surface of the organism is advantageous to facilitate the oxidative fermentation of the cyclic alcohols. Since cyclic alcohols have some biological toxicity to living cells, according to the mechanism of the oxidative fermentation, there is no need to incorporate such toxic compounds into the cytoplasm
-
brenda
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moonmangmee, D.; Fujii, Y.; Toyama, H.; Theeragool, G.; Lotong, N.; Matsushita, K.; Adachi, O.
Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM 9
Biosci. Biotechnol. Biochem.
65
2763-2772
2001
Gluconobacter frateurii, Gluconobacter frateurii CHM 9
brenda
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Release 2023.1 (January 2023)
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