EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.23 | 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 | ? | - |
? | |
1.14.15.15 | 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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.23 | Mycolicibacterium smegmatis | - |
gene CYP125A4 | - |
1.14.15.15 | Mycolicibacterium smegmatis | - |
gene CYP125A4 | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.14.23 | culture condition:cholesterol-grown cell | Mycobacterium smegmatis can grow on cholesterol as the sole carbon source | Mycolicibacterium smegmatis | - |
1.14.15.15 | culture condition:cholesterol-grown cell | Mycobacterium smegmatis can grow on cholesterol as the sole carbon source | Mycolicibacterium smegmatis | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.23 | 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 | ? | - |
? | |
1.14.15.15 | 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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.14.23 | CYP125A4 | - |
Mycolicibacterium smegmatis |
1.14.14.23 | cytochrome P450 125A4 | - |
Mycolicibacterium smegmatis |
1.14.14.23 | More | cf. EC 1.14.15.15 | Mycolicibacterium smegmatis |
1.14.15.15 | cholesterol C-26 hydroxylase | - |
Mycolicibacterium smegmatis |
1.14.15.15 | CYP125A4 | - |
Mycolicibacterium smegmatis |
1.14.15.15 | cytochrome P450 125A4 | - |
Mycolicibacterium smegmatis |
1.14.15.15 | More | cf. EC 1.14.14.23 | Mycolicibacterium smegmatis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.14.23 | 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 |
1.14.14.23 | 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 |
1.14.15.15 | 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 |
1.14.15.15 | 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 |