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Literature summary for 1.1.3.6 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
Search for more literature for 1.1.3.6

Cloned(Commentary)

Cloned (Comment) Organism
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

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

KM Value [mM]

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

Localization

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cholesterol + O2
-
 Mycolicibacterium neoaurum cholest-4-en-3-one + H2O2
-
 ?
cholesterol + O2
-
 Mycolicibacterium neoaurum JC-12 cholest-4-en-3-one + H2O2
-
 ?
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 ?
-
 ?
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

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

Synonyms

Synonyms Comment Organism
CHO
-
 Mycolicibacterium neoaurum
choM
-
 Mycolicibacterium neoaurum
ChoM1
-
 Mycolicibacterium neoaurum
ChoM2
-
 Mycolicibacterium neoaurum

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Mycolicibacterium neoaurum

Cofactor

Cofactor Comment Organism Structure
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
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

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