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Literature summary extracted from

  • Siegel, L.M.; Leinweber, F.J.; Monty, K.J.
    Characterization of the sulfite and hydroxylamine reductases of Neurospora crassa (1965), J. Biol. Chem., 240, 2705-2711.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.1.10 sulfite uncompetitive vs. hydroxylamine Neurospora crassa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.1.10 hydroxylamine + NADH Neurospora crassa involved in pathway of nitrate reduction NH3 + NAD+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.7.1.10 Neurospora crassa
-
 3 hydroxylamine reductases: one is identical with sulfite reductase and is absolutely specific for NADPH, accepts hydroxylamine and sulfate as substrates at a common binding site, a second hydroxylamine reductase uses either NADH or NADPH and is stimulated by FAD, a third hydroxylamine reductase is also able to accept NADH and NADPH
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.1.10 hydroxylamine + NADH NADPH is 2fold more effective than NADH Neurospora crassa NH3 + NAD+ + H2O
-
 ?
1.7.1.10 hydroxylamine + NADH involved in pathway of nitrate reduction Neurospora crassa NH3 + NAD+ + H2O
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.1.10 NADH
-
 Neurospora crassa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.7.1.10 0.7
-
 sulfite
-
 Neurospora crassa