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Literature summary extracted from

  • Trudgill, P.W.
    Cyclohexanone 1,2-monooxygenase from Acinetobacter NCIMB 9871 (1990), Methods Enzymol., 188, 70-77.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.22 7-Chloro-8-demethyl-FAD reactivates apoenzyme Acinetobacter sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.22 5,5'-dithiobis(2-nitrobenzoate)
-
Acinetobacter sp.
1.14.13.22 5-deaza-FAD competitive Acinetobacter sp.
1.14.13.22 p-hydroxymercuribenzoate
-
Acinetobacter sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.22 0.004
-
cyclohexanone
-
Acinetobacter sp.
1.14.13.22 0.02
-
NADPH
-
Acinetobacter sp.
1.14.13.22 3.6
-
Cyclopentanone
-
Acinetobacter sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.22 cyclohexanone + NADPH + O2 Acinetobacter sp. enzyme plays an important role in degradation of keto-compounds by microorganisms 1-oxa-2-oxocycloheptane + NADP+ + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.22 Acinetobacter sp.
-
NCIB 9871
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.22
-
Acinetobacter sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.22 cyclohexanone + NADPH + H+ + O2 = hexano-6-lactone + NADP+ + H2O ter-ter mechanism Acinetobacter sp.
1.14.13.22 cyclohexanone + NADPH + H+ + O2 = hexano-6-lactone + NADP+ + H2O a stable 4a-hydroperoxy-flavin carries out a nucleophilic attack on the ketone Acinetobacter sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.13.22 2.1
-
-
Acinetobacter sp.

Storage Stability

EC Number Storage Stability Organism
1.14.13.22 -20°C, more than 1 year Acinetobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.22 (+)-camphor + NADPH + O2
-
Acinetobacter sp. ?
-
?
1.14.13.22 2-methylcyclohexanone + NADPH + O2
-
Acinetobacter sp. 1-oxa-2-oxo-3-methylcycloheptane + NADP+ + H2O
-
?
1.14.13.22 4-methylcyclohexanone + NADPH + O2
-
Acinetobacter sp. 1-oxa-2-oxo-5-methylcycloheptane + NADP+ + H2O
-
?
1.14.13.22 cyclobutanone + NADPH + O2
-
Acinetobacter sp. 1-oxa-2-oxo-cyclopentane + NADP+ + H2O
-
?
1.14.13.22 cycloheptanone + NADPH + O2
-
Acinetobacter sp. 1-oxa-2-oxo-cyclooctane + NADP+ + H2O
-
?
1.14.13.22 cyclohexanone + NADPH + O2
-
Acinetobacter sp. 6-hexanolide + NADP+ + H2O product: epsilon-caprolactone i.e. 1-oxa-2-oxocycloheptane ?
1.14.13.22 cyclohexanone + NADPH + O2 enzyme plays an important role in degradation of keto-compounds by microorganisms Acinetobacter sp. 1-oxa-2-oxocycloheptane + NADP+ + H2O
-
?
1.14.13.22 cyclooctanone + NADPH + O2
-
Acinetobacter sp. 1-oxa-2-oxo-cyclononane + NADP+ + H2O
-
?
1.14.13.22 cyclopentanone + NADPH + O2
-
Acinetobacter sp. 1-oxa-2-oxo-cyclohexane + NADP+ + H2O
-
?
1.14.13.22 dihydrocarvone + NADPH + O2
-
Acinetobacter sp. ?
-
?
1.14.13.22 additional information absolutely specific for NADPH as electron donor Acinetobacter sp. ?
-
?
1.14.13.22 norcamphor + NADPH + O2
-
Acinetobacter sp. ?
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.22 9
-
-
Acinetobacter sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.22 6-Methyl-FAD reactivates apoenzyme Acinetobacter sp.
1.14.13.22 9-Aza-FAD reactivates apoenzyme Acinetobacter sp.
1.14.13.22 FAD
-
Acinetobacter sp.
1.14.13.22 NADPH electron donor Acinetobacter sp.
1.14.13.22 NADPH absolutely specific for NADPH as electron donor Acinetobacter sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.13.22 0.062
-
5-deaza-FAD
-
Acinetobacter sp.