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Literature summary extracted from
- Single or multiple access channels to the CYP450s active site? An answer from free energy simulations of the human aromatase enzyme (2017), J. Phys. Chem. Lett., 8, 2036-2042 .
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.14.14 | free energy simulations of the entry/exit routes preferentially followed by substrate androstenedione and inhibitor letrozole. Two channels appear accessible to their entrance, while only one exit route appears to be preferential, ligand channeling is associated with large enzyme structural rearrangements | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.14 | letrozole | - |
Homo sapiens |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.14 | Homo sapiens | P11511 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.14 | androst-4-ene-3,17-dione + 3 O2 + 3 reduced flavoproteins | - |
Homo sapiens | estrone + formate + 4 H2O + 3 oxidized flavoproteins | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.14 | CYP19A1 | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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