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 | 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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | mainly | Mycolicibacterium neoaurum | - |
- |
intracellular | - |
Mycolicibacterium neoaurum | 5622 | - |
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 | 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 | 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 (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 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 | 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 | 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 | Comment | Organism |
---|---|---|
CHO | - |
Mycolicibacterium neoaurum |
choM | - |
Mycolicibacterium neoaurum |
ChoM1 | - |
Mycolicibacterium neoaurum |
ChoM2 | - |
Mycolicibacterium neoaurum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
- |
Mycolicibacterium neoaurum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Mycolicibacterium neoaurum |
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 | 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 |