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Literature summary extracted from

  • Secundo, F.; Zambianchi, F.; Crippa, G.; Carrea, G.; Tedeschi, G.
    Comparative study of the properties of wild type and recombinant cyclohexanone monooxygenase, an enzyme of synthetic interest (2005), J. Mol. Catal. B, 34, 1-6.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.22 additional information the enzyme is inducible by cyclohexanone Acinetobacter calcoaceticus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.22 expression in Escherichia coli under control of a strong L-arabinose inducible promoter Acinetobacter calcoaceticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.22 0.0014
-
 bicyclo[3.2.0]hept-2-en-6-one pH 8.6, 25°C, recombinant and native enzyme Acinetobacter calcoaceticus

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 calcoaceticus
-
 hexano-6-lactone + NADP+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.22 Acinetobacter calcoaceticus
-
 an inducible enzyme
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.22 recombinant enzyme 21fold from Escherichia coli and native enzyme to homogeneity by ion exchange and affinity chromatography Acinetobacter calcoaceticus

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 9.1
-
 purified recombinant enzyme, substrate bicyclo[3.2.0]hept-2-en-6-one Acinetobacter calcoaceticus
1.14.13.22 9.2
-
 purified native enzyme, substrate bicyclo[3.2.0]hept-2-en-6-one Acinetobacter calcoaceticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.22 bicyclo[3.2.0]hept-2-en-6-one + NADPH + O2
-
 Acinetobacter calcoaceticus ?
-
 ?
1.14.13.22 cyclohexanone + NADPH + O2
-
 Acinetobacter calcoaceticus hexano-6-lactone + NADP+ + H2O
-
 ?
1.14.13.22 additional information the enzyme catalyses the NADPH-dependent enantioselective oxidation of ketones and of several heteroatoms such as nitrogen, sulfur, phosphorous and selenium present in organic compounds Acinetobacter calcoaceticus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.22 ? x * 61586.04, recombinant enzyme, mass spectrometry, x * 61583.54, native enzyme, mass spectrometry Acinetobacter calcoaceticus

Synonyms

EC Number Synonyms Comment Organism
1.14.13.22 CHMO
-
 Acinetobacter calcoaceticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.22 25
-
 assay at Acinetobacter calcoaceticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.22 8.6
-
 assay at Acinetobacter calcoaceticus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.14.13.22 additional information
-
 comparison of pH stability of crude, partially purified, and purified native and recombinant enzymes, overview Acinetobacter calcoaceticus
1.14.13.22 6
-
 48 h, purified recombinant enzyme: loss of 12% activity, native enzyme: loss of 24% activity Acinetobacter calcoaceticus
1.14.13.22 8.6
-
 48 h, purified recombinant enzyme: loss of 15% activity, native enzyme: loss of 24% activity Acinetobacter calcoaceticus
1.14.13.22 10
-
 48 h, purified recombinant enzyme: loss of 45% activity, native enzyme: loss of 82% activity Acinetobacter calcoaceticus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.22 FAD flavoenzyme Acinetobacter calcoaceticus
1.14.13.22 NADPH dependent on Acinetobacter calcoaceticus