Activating Compound | Comment | Organism | Structure |
---|---|---|---|
cytochrome b5 | presence of cytochrome b5 markedly stimulates the 17,20-lyase reaction, with little effect on 17-hydroxylation. For the 17-hydroxylase reaction, progesterone oxidation is the most tightly coupled (about 50%) and negligibly changed upon addition of b5. For the 17,20-lyase reactions, b5 markedly increases product formation and coupling in parallel with all substrates, from 6% to 44% with the major substrate 17-hydroxypregnenolone | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
- |
Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
E305G | naturally occurring P450 17A1 mutation, impairs 17,20-lyase activity. Cytochrome b5 fails to rescue the poor coupling with 17-hydroxypregnenolone | Homo sapiens |
R347H | naturally occurring P450 17A1 mutation, impairs 17,20-lyase activity. Cytochrome b5 fails to rescue the poor coupling with 17-hydroxypregnenolone | Homo sapiens |
T306A | mutation in the conserved active-site threonine, both the activity and coupling are markedly decreased with all substrates | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P05093 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
17alpha-hydroxypregnenolone + [reduced NADPH-hemoprotein reductase] + O2 | - |
Homo sapiens | 3beta-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
17alpha-hydroxyprogesterone + [reduced NADPH-hemoprotein reductase] + O2 | - |
Homo sapiens | androstenedione + acetate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
allopregnanolone + [reduced NADPH-hemoprotein reductase] + O2 | - |
Homo sapiens | androstenedione + acetate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cytochrome P450 17A1 | - |
Homo sapiens |