Literature summary for 1.7.1.10 extracted from

Bernheim, M.L.C.; Hochstein, P.
Reduction of hydroxylamine by rat liver mitochondria (1968), Arch. Biochem. Biophys., 124, 436-442.

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Inhibitors

Inhibitors	Comment	Organism	Structure
HgCl2	1 mM, complete inhibition	Rattus norvegicus
KCN	-	Rattus norvegicus
N-ethylmaleimide	1 mM, 50% inhibition	Rattus norvegicus
p-chloromercuribenzoate	1 mM, complete inhibition	Rattus norvegicus
p-hydroxymercuribenzoate	-	Rattus norvegicus
phosphate	-	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Rattus norvegicus	5739	-

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Rattus norvegicus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
hydroxylamine + NADH	enzyme also reduces anthranilic hydroxamic acid and nicotinic hydroxamic acid, affinity is about twenty times lower than for hydroxylamine	Rattus norvegicus	NH3 + NAD+ + H2O	-	?
hydroxylamine + NADH	NADH is 1.5fold more effective than NADPH	Rattus norvegicus	NH3 + NAD+ + H2O	-	?

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
27	-	stable for more than 1 h	Rattus norvegicus
38	-	1 h, inactivation	Rattus norvegicus

pH Range

pH Minimum	pH Maximum	Comment	Organism
5.4	8.4	pH 5.4: considerable activity in Tris-maleate buffer, pH 8.4: about 50% activity	Rattus norvegicus
5.5	7.2	pH 5.5: about 70% of activity maximum, pH 7.2: 50% activity	Rattus norvegicus

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Rattus norvegicus
NADPH	about 65% of the activity with NADH	Rattus norvegicus

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Release 2023.1 (January 2023)