EC 1.1.5.7: cyclic alcohol dehydrogenase (quinone)
This is an abbreviated version!
For detailed information about cyclic alcohol dehydrogenase (quinone), go to the full flat file.
Reaction
Synonyms
MCAD
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Substrates Products
Substrates Products on EC 1.1.5.7 - cyclic alcohol dehydrogenase (quinone)
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REACTION DIAGRAM
(1R,2R)-trans-1,2-cyclohexanediol + pyrroloquinoline quinone
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Substrates: 74% of the activity compared to cyclopentanol
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(1S,2S)-trans-1,2-cyclohexanediol + pyrroloquinoline quinone
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Substrates: 11% of the activity compared to cyclopentanol
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(2R,3R)-2,3-butanediol + pyrroloquinoline quinone
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Substrates: 41% of the activity compared to cyclopentanol
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1,2-butanediol + pyrroloquinoline quinone
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Substrates: 63% of the activity compared to cyclopentanol
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1,3-butanediol + pyrroloquinoline quinone
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Substrates: 12% of the activity compared to cyclopentanol
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1,3-cyclopentanediol + pyrroloquinoline quinone
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Substrates: 73% of the activity compared to cyclopentanol
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1,4-cyclohexanediol + pyrroloquinoline quinone
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Substrates: 14% of the activity compared to cyclopentanol
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2,3-butanediol + pyrroloquinoline quinone
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Substrates: 186% of the activity compared to cyclopentanol
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2,4-pentanediol + pyrroloquinoline quinone
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Substrates: 16% of the activity compared to cyclopentanol
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2-butanol + pyrroloquinoline quinone
butane-2-one + reduced pyrroloquinoline quinone
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Substrates: 41% of the activity compared to cyclopentanol
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2-hexanol + pyrroloquinoline quinone
2-hexanone + pyrroloquinoline quinol
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Substrates: 10% of the activity compared to cyclopentanol
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2-methyl-2,4-pentanediol + pyrroloquinoline quinone
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Substrates: 17% of the activity compared to cyclopentanol
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2-propanol + pyrroloquinoline quinone
acetone + pyrroloquinoline quinol
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Substrates: 17% of the activity compared to cyclopentanol
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3-pentanol + pyrroloquinoline quinone
3-pentanone + pyrroloquinoline quinol
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Substrates: 74% of the activity compared to cyclopentanol
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cis-1,2-cyclohexanediol + pyrroloquinoline quinone
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Substrates: 88% of the activity compared to cyclopentanol
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cis-1,2-cyclopentanediol + pyrroloquinoline quinone
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Substrates: 181% of the activity compared to cyclopentanol
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cis-4-cyclopentene-1,3-diol + pyrroloquinoline quinone
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Substrates: 32% of the activity compared to cyclopentanol
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D-arabitol + pyrroloquinoline quinone
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Substrates: 78% of the activity compared to cyclopentanol
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D-mannitol + pyrroloquinoline quinone
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Substrates: 25% of the activity compared to cyclopentanol
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D-sorbitol + pyrroloquinoline quinone
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Substrates: 34% of the activity compared to cyclopentanol
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glycerol + pyrroloquinoline quinone
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Substrates: 59% of the activity compared to cyclopentanol
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meso-erythritol + pyrroloquinoline quinone
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Substrates: 100% of the activity compared to cyclopentanol
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ribitol + pyrroloquinoline quinone
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Substrates: 34% of the activity compared to cyclopentanol
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cyclobutanone + pyrroloquinoline quinol
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Substrates: 73% of the activity compared to cyclopentanol
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cyclobutanol + pyrroloquinoline quinone
cyclobutanone + pyrroloquinoline quinol
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Substrates: 73% of the activity compared to cyclopentanol
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cyclohexanone + pyrroloquinoline quinol
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Substrates: 73% of the activity compared to cyclopentanol
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cyclohexanol + pyrroloquinoline quinone
cyclohexanone + pyrroloquinoline quinol
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Substrates: 73% of the activity compared to cyclopentanol
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cyclooctanone + pyrroloquinoline quinol
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Substrates: 137% of the activity compared to cyclopentanol
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cyclooctanol + pyrroloquinoline quinone
cyclooctanone + pyrroloquinoline quinol
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Substrates: 137% of the activity compared to cyclopentanol
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cyclopentanone + pyrroloquinoline quinol
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Substrates: only pyrroloquinoline quinone is effective as electron acceptor, no activity with FAD, FMN and NAD(P)+
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cyclopentanol + pyrroloquinoline quinone
cyclopentanone + pyrroloquinoline quinol
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Substrates: only pyrroloquinoline quinone is effective as electron acceptor, no activity with FAD, FMN and NAD(P)+
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Substrates: 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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additional information
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Substrates: 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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additional information
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Substrates: 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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