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Literature summary for 1.14.13.22 extracted from

  • Latham, J.A.; Walsh, C.
    Retention of configuration in oxidation of a chiral boronic acid by the flavoenzyme cyclihexanone oxygenase (1986), J. Chem. Soc. Chem. Commun., 1986, 527-528.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Acinetobacter sp.
0.07
-
2-methylcyclohexyl boronic acid
-
Acinetobacter sp.

Organism

Organism UniProt Comment Textmining
Acinetobacter sp.
-
NCIB 9871
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-methylcyclohexyl boronic acid + NADPH + O2 racemic substrate Acinetobacter sp. 2-methylcyclohexanol + BO3- + NADP+ + H2O
-
?
additional information peroxide-like oxidation catalyzed Acinetobacter sp. ?
-
?
additional information ability to convert aryl and alkyl boronic acids into phenols and alcohols, racemic 2-methylcyclohexyl boronic acid is processed to 2-methylcyclohexanol Acinetobacter sp. ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Acinetobacter sp.
8.4
-
2-methylcyclohexyl boronic acid
-
Acinetobacter sp.

Cofactor

Cofactor Comment Organism Structure
FAD enzyme-bound FAD-4a-OOH is the actual oxygenation reagent Acinetobacter sp.
NADPH
-
Acinetobacter sp.