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Literature summary for 1.14.13.22 extracted from

  • Ryerson, C.C.; Ballou, D.P.; Walsh, C.
    Mechanistic studies on cyclohexanone oxygenase (1982), Biochemistry, 21, 2644-2655.
    View publication on PubMed
Search for more literature for 1.14.13.22

Activating Compound

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

Inhibitors

Inhibitors Comment Organism Structure
5-deaza-FAD competitive Acinetobacter sp.
NADP+ competitive against NADPH Acinetobacter sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
 NADPH
-
 Acinetobacter sp.
0.024
-
 Thiane
-
 Acinetobacter sp.
0.1
-
 O2 below Acinetobacter sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
 native PAGE Acinetobacter sp.

Organism

Organism UniProt Comment Textmining
Acinetobacter sp.
-
 NCIB 9871
-

Purification (Commentary)

Purification (Comment) Organism
-
 Acinetobacter sp.

Reaction

Reaction Comment Organism Reaction ID
cyclohexanone + NADPH + H+ + O2 = hexano-6-lactone + NADP+ + H2O reaction mechanism Acinetobacter sp.
a
cyclohexanone + NADPH + H+ + O2 = hexano-6-lactone + NADP+ + H2O mechanistic study Acinetobacter sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclohexanone + NADPH + O2
-
 Acinetobacter sp. 6-hexanolide + NADP+ + H2O product: epsilon-caprolactone i.e. 1-oxa-2-oxocycloheptane ?
thiane + NADPH + O2
-
 Acinetobacter sp. ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 56000, SDS-PAGE Acinetobacter sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at 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.
30.3
-
 cyclohexanone
-
 Acinetobacter sp.

Cofactor

Cofactor Comment Organism Structure
1-deaza-FAD reactivates apoenzyme Acinetobacter sp.
9-Aza-FAD reactivates apoenzyme Acinetobacter sp.
FAD reactivates apoenzyme Acinetobacter sp.
NADPH
-
 Acinetobacter sp.

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.038
-
 NADP+
-
 Acinetobacter sp.
0.062
-
 5-deaza-FAD
-
 Acinetobacter sp.