Literature summary for 1.7.1.10 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.

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Inhibitors

Inhibitors	Comment	Organism	Structure
sulfite	uncompetitive vs. hydroxylamine	Neurospora crassa

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
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)

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

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Neurospora crassa

Ki Value [mM]

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

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Release 2023.1 (January 2023)