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Literature summary for 1.6.2.4 extracted from
- Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase (2007), Biochemistry, 46, 12212-12219.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Rattus norvegicus | the C-terminal 23 amino acids of heme oxygenase-1 play an important role in the interaction between heme oxygenase-1 and NADPH cytochrome P450 reductase, enhancing the conversion of hemin to biliverdin | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
recombinant | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the C-terminal 23 amino acids of heme oxygenase-1 play an important role in the interaction between heme oxygenase-1 and NADPH cytochrome P450 reductase, enhancing the conversion of hemin to biliverdin | Rattus norvegicus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CPR | - |
Rattus norvegicus |
| NADPH cytochrome P450 reductase | - |
Rattus norvegicus |
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Release 2023.1 (January 2023)
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