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Literature summary for 1.7.1.10 extracted from
- Properties of a NADH-dependent N-hydroxy amine reductase isolated from pig liver microsomes (1974), Arch. Biochem. Biophys., 162, 83-92.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microsome | - |
Sus scrofa | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
microsomal multicomponent enzyme system consisting of NADH, cytochrome b5, cytochrome b5 reductase and a third unidentified protein, catalyzes reduction of hydroxylamine and a number of its mono- and disubstituted derivatives | - |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| very unstable in the absence of sulfhydryl protecting agents, stable in the presence of 0.2 mM dithiothreitol | Sus scrofa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Sus scrofa | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hydroxylamine + NADH | 30-40% activity with NADPH | Sus scrofa | NH3 + NAD+ + H2O | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | 3 protein fractions are required to reconstitute NADH-hydroxylamine reductase activity: detergent-extracted cytochrome b5 and its flavoprotein and a third microsomal protein | Sus scrofa |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Sus scrofa | |
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Release 2023.1 (January 2023)
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