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Literature summary 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

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.1.10 microsome
-
 Sus scrofa
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.7.1.10 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

EC Number Oxidation Stability Organism
1.7.1.10 very unstable in the absence of sulfhydryl protecting agents, stable in the presence of 0.2 mM dithiothreitol Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.7.1.10 liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.1.10 hydroxylamine + NADH 30-40% activity with NADPH Sus scrofa NH3 + NAD+ + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.1.10 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

EC Number Cofactor Comment Organism Structure
1.7.1.10 NADH
-
 Sus scrofa