Any feedback?
Literature summary for 1.14.14.19 extracted from
- The use of random chimeragenesis to study structure/function properties of rat and human P450c17 (2000), Arch. Biochem. Biophys., 373, 401-408.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli JM109, human gene with an (His)4-tail | Homo sapiens |
| expression in Escherichia coli JM109, human gene with an (His)4-tail | Rattus norvegicus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | it catalyzes steroid 17alpha-hydroxylase and 17,20-lyase activities in the biosynthesis of androgens, estrogens and cortisol | ? | - |
? |  |
| additional information | Rattus norvegicus | it catalyzes steroid 17alpha-hydroxylase and 17,20-lyase activities in the biosynthesis of androgens, estrogens and cortisol | ? | - |
? | |
| pregnenolone + AH2 + O2 | Homo sapiens | - |
17alpha-hydroxypregnenolone + A + H2O | product eliminates at C20,21 acetate to yield dehydroepiandrosterone | ? | |
| pregnenolone + AH2 + O2 | Rattus norvegicus | - |
17alpha-hydroxypregnenolone + A + H2O | product eliminates at C20,21 acetate to yield dehydroepiandrosterone | ? | |
| progesterone + [reduced NADPH-hemoprotein reductase] + O2 | Homo sapiens | - |
17alpha-hydroxyprogesterone + [oxidized NADPH-hemoprotein reductase] + H2O | product eliminates at C20,21 acetate to yield androstenedione | ? | |
| progesterone + [reduced NADPH-hemoprotein reductase] + O2 | Rattus norvegicus | - |
17alpha-hydroxyprogesterone + [oxidized NADPH-hemoprotein reductase] + H2O | product eliminates at C20,21 acetate to yield androstenedione | ? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | it catalyzes steroid 17alpha-hydroxylase and 17,20-lyase activities in the biosynthesis of androgens, estrogens and cortisol | Homo sapiens | ? | - |
? | |
| additional information | it catalyzes steroid 17alpha-hydroxylase and 17,20-lyase activities in the biosynthesis of androgens, estrogens and cortisol | Rattus norvegicus | ? | - |
? | |
| pregnenolone + AH2 + O2 | - |
Homo sapiens | 17alpha-hydroxypregnenolone + A + H2O | product eliminates at C20,21 acetate to yield dehydroepiandrosterone | ? | |
| pregnenolone + AH2 + O2 | - |
Rattus norvegicus | 17alpha-hydroxypregnenolone + A + H2O | product eliminates at C20,21 acetate to yield dehydroepiandrosterone | ? | |
| progesterone + [reduced NADPH-hemoprotein reductase] + O2 | - |
Homo sapiens | 17alpha-hydroxyprogesterone + [oxidized NADPH-hemoprotein reductase] + H2O | product eliminates at C20,21 acetate to yield androstenedione | ? | |
| progesterone + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rattus norvegicus | 17alpha-hydroxyprogesterone + [oxidized NADPH-hemoprotein reductase] + H2O | product eliminates at C20,21 acetate to yield androstenedione | ? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| P450c17 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
- |
Homo sapiens |
| 37 | - |
- |
Rattus norvegicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Homo sapiens |
| 7.2 | - |
assay at | Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADPH | - |
Homo sapiens | |
| NADPH | - |
Rattus norvegicus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
