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Literature summary for 5.3.99.5 extracted from
- Comparison of the construction of a 3-D model for human thromboxane synthase using P450cam and BM-3 as templates: implications for the substrate binding pocket (1994), Protein Eng., 7, 1345-1351.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Prostaglandin H2 | i.e. PGH2 | Homo sapiens | thromboxane B2 + 12(L)-hydroxy-5,8,10-heptadecatrienoic acid | - |
? |  |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | hemoprotein | Homo sapiens | |
| heme | comparison of thromboxane A2 synthase model based on the P450BM-3 with another thromboxane A2 synthase model based on the P450cam structure indicates that P450BM-3 is a more suitable template for homology modeling of thromboxane A2 synthase. P450BM-3 and p450cam are hemoprotein domains of cytochrome | Homo sapiens | |
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Release 2023.1 (January 2023)
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