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Literature summary extracted from

  • Shao, M.; Rao, Z.; Zhang, X.; Xu, M.; Yang, T.; Li, H.; Xu, Z.; Yang, S.
    Bioconversion of cholesterol to 4-cholesten-3-one by recombinant Bacillus subtilis expressing choM gene encoding cholesterol oxidase from Mycobacterium neoaurum JC-12 (2015), J. Chem. Technol. Biotechnol., 90, 1811-1820 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.6 gene choM, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His-tagged isozyme in Bacillus subtilis strain 168/pMA5 mainly intracellularly Mycolicibacterium neoaurum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.6 Ag+
-
 Mycolicibacterium neoaurum
1.1.3.6 Al3+
-
 Mycolicibacterium neoaurum
1.1.3.6 Cu2+
-
 Mycolicibacterium neoaurum
1.1.3.6 Fe2+
-
 Mycolicibacterium neoaurum
1.1.3.6 Fe3+
-
 Mycolicibacterium neoaurum
1.1.3.6 Hg2+
-
 Mycolicibacterium neoaurum
1.1.3.6 Zn2+
-
 Mycolicibacterium neoaurum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.6 additional information
-
 additional information Michaelis-Menten kinetics Mycolicibacterium neoaurum
1.1.3.6 0.13
-
 cholesterol pH 7.5, 40°C, recombinant isozyme ChoM1 Mycolicibacterium neoaurum
1.1.3.6 0.16
-
 cholesterol pH 7.5, 40°C, recombinant isozyme ChoM1 Mycolicibacterium neoaurum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.3.6 extracellular mainly Mycolicibacterium neoaurum
-
-
1.1.3.6 intracellular
-
 Mycolicibacterium neoaurum 5622
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.3.6 Mg2+ activates 58% at 1 mM Mycolicibacterium neoaurum
1.1.3.6 Mn2+ activates Mycolicibacterium neoaurum
1.1.3.6 additional information no or poor effects by Na+, K+, Ni2+, and Ca2+, and EDTA Mycolicibacterium neoaurum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.6 cholesterol + O2 Mycolicibacterium neoaurum
-
 cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Mycolicibacterium neoaurum JC-12
-
 cholest-4-en-3-one + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.6 Mycolicibacterium neoaurum H9NJ43 isozyme ChoM1
-
1.1.3.6 Mycolicibacterium neoaurum H9NJ52 isozyme ChoM2; isolated from the environment, China
-
1.1.3.6 Mycolicibacterium neoaurum JC-12 H9NJ43 isozyme ChoM1
-
1.1.3.6 Mycolicibacterium neoaurum JC-12 H9NJ52 isozyme ChoM2; isolated from the environment, China
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.6 recombinant His-tagged isozyme CHOM1 from Bacillus subtilis strain 168/pMA5 by nickel affinity chromatography Mycolicibacterium neoaurum
1.1.3.6 recombinant His-tagged isozyme CHOM2 from Bacillus subtilis strain 168/pMA5 by nickel affinity chromatography Mycolicibacterium neoaurum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.3.6 0.24
-
 native crude enzyme intracellular in strain JC-12, both ChoM isozymes, pH 7.5, 40°C Mycolicibacterium neoaurum
1.1.3.6 0.78
-
 native crude enzyme extracellular in strain JC-12, both ChoM isozymes, pH 7.5, 40°C Mycolicibacterium neoaurum
1.1.3.6 11.2
-
 purified recombinant His-tagged isozyme ChoM1, pH 7.5, 40°C Mycolicibacterium neoaurum
1.1.3.6 17.2
-
 purified recombinant His-tagged isozyme ChoM2, pH 7.5, 40°C Mycolicibacterium neoaurum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.6 cholesterol + O2
-
 Mycolicibacterium neoaurum cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Mycolicibacterium neoaurum JC-12 cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 additional information the bifunctional FAD-dependent enzyme catalyzes the oxidation and isomerization of sterols to sterones, typically cholesterol (5-cholesten-3-beta-ol) to 4-cholesten-3-one (cholestenone) and H2O2. The enzyme shows higher activity towards the 3beta-hydroxy steroids with long alkyl chains at C17 Mycolicibacterium neoaurum ?
-
 ?
1.1.3.6 additional information the bifunctional FAD-dependent enzyme catalyzes the oxidation and isomerization of sterols to sterones, typically cholesterol (5-cholesten-3-beta-ol) to 4-cholesten-3-one (cholestenone) and H2O2. The enzyme shows higher activity towards the 3beta-hydroxy steroids with long alkyl chains at C17 Mycolicibacterium neoaurum JC-12 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.3.6 ? x * 58800, recombinant His-tagged isoyzme ChoM2, SDS-PAGE Mycolicibacterium neoaurum
1.1.3.6 ? x * 64100, recombinant His-tagged isoyzme ChoM1, SDS-PAGE Mycolicibacterium neoaurum

Synonyms

EC Number Synonyms Comment Organism
1.1.3.6 CHO
-
 Mycolicibacterium neoaurum
1.1.3.6 choM
-
 Mycolicibacterium neoaurum
1.1.3.6 ChoM1
-
 Mycolicibacterium neoaurum
1.1.3.6 ChoM2
-
 Mycolicibacterium neoaurum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.6 40
-
-
 Mycolicibacterium neoaurum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.6 7.5
-
-
 Mycolicibacterium neoaurum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.6 FAD isozyme ChoM1 contains a typical consensus sequence (GXGXXGXXXAXXXXXXG) in the FAD-binding site, which is located near the N-terminal end at amino acids 11-27 Mycolicibacterium neoaurum
1.1.3.6 FAD isozyme ChoM2 contains a typical consensus sequence (GXGXXGXXXAXXXXXXG) in the FAD-binding site, which is located near the N-terminal end at amino acids 45-61 Mycolicibacterium neoaurum

General Information

EC Number General Information Comment Organism
1.1.3.6 additional information key amino acid residues involved in substrate oxidation are His470 and Asn513 in ChoM1 Mycolicibacterium neoaurum
1.1.3.6 additional information key amino acid residues involved in substrate oxidation are His479 and Asn517 in ChoM1 Mycolicibacterium neoaurum