Any feedback?
Literature summary for 1.14.14.18 extracted from
- The oxidation of hemins by microsomal heme oxygenase. Structural requirements for the retention of substrate activity (1984), Biochim. Biophys. Acta, 791, 342-349.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microsome | - |
Rattus norvegicus | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| heme + electron donor + O2 | overview, substrate specificity | Rattus norvegicus | biliverdin + Fe2+ + CO + oxidized eletron donor + H2O | - |
? |  |
| heme + electron donor + O2 | synthetic hemins XIII and III and iron porphyrin are better substrates than the natural substrate hemin IX, 83 and 86% of hemin IX activity with mesohemin IX and hematohemin IX respectively | Rattus norvegicus | biliverdin + Fe2+ + CO + oxidized eletron donor + H2O | - |
? | |
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
