Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mycolicibacterium smegmatis | enzyme CYP125A4 also oxidizes cholesterol, although it has a much higher activity for the oxidation of 7alpha-hydroxycholesterol, EC 1.14.14.23. The enzyme forms 7alpha,26-dihydroxycholesterol | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycolicibacterium smegmatis | - |
gene CYP125A4 | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
culture condition:cholesterol-grown cell | Mycobacterium smegmatis can grow on cholesterol as the sole carbon source | Mycolicibacterium smegmatis | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | enzyme CYP125A4 also oxidizes cholesterol, although it has a much higher activity for the oxidation of 7alpha-hydroxycholesterol, EC 1.14.14.23. The enzyme forms 7alpha,26-dihydroxycholesterol | Mycolicibacterium smegmatis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CYP125A4 | - |
Mycolicibacterium smegmatis |
cytochrome P450 125A4 | - |
Mycolicibacterium smegmatis |
More | cf. EC 1.14.15.15 | Mycolicibacterium smegmatis |
General Information | Comment | Organism |
---|---|---|
additional information | the ability of CYP125A4 to oxidize 7alpha-hydroxycholesterol is due, at least in part, to the presence of a smaller amino acid side chain facing C-7 of the sterol substrate than in CYP125A3 | Mycolicibacterium smegmatis |
physiological function | utilization of cholesterol is initiated by three cholesterol hydroxylases, CYP125A3, CYP142A2, and CYP125A4. A CYP125A3/CYP142A2 double knockout mutant of Mycobacterium smegmatis is still able to grow on cholesterol as sole carbom source, albeit at a slower rate than the wild-type | Mycolicibacterium smegmatis |