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Literature summary for extracted from

  • Kadlubar, F.F.; Ziegler, D.M.
    Properties of a NADH-dependent N-hydroxy amine reductase isolated from pig liver microsomes (1974), Arch. Biochem. Biophys., 162, 83-92.
    View publication on PubMed


Localization Comment Organism GeneOntology No. Textmining
Sus scrofa


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
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 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 Comment Organism Structure
Sus scrofa