EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.80 | cytochrome b5 | stimulates steady-state lauric acid omega-hydroxylation about 2fold | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.80 | lauric acid + [reduced NADPH-hemoprotein reductase] + O2 + H+ | Homo sapiens | - |
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
1.14.14.80 | additional information | Homo sapiens | substrate and product binding and release are much faster than overall rates of catalysis. Both the transfer of an electron to the ferrous-O2 complex and C-H bond-breaking limit the rate of P450 4A11 omega-oxidation | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.80 | Homo sapiens | Q02928 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.80 | lauric acid + [reduced NADPH-hemoprotein reductase] + O2 + H+ | - |
Homo sapiens | 12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
1.14.14.80 | additional information | substrate and product binding and release are much faster than overall rates of catalysis. Both the transfer of an electron to the ferrous-O2 complex and C-H bond-breaking limit the rate of P450 4A11 omega-oxidation | Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.14.80 | cytochrome P450 4A11 | - |
Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.80 | cytochrome P450 | reduction of ferric P450 4A11 to ferrous is rapid and not rate-limiting | Homo sapiens |