Hydroxylamine oxidase
hydroxylamine oxidase | |||||||||
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Identifiers | |||||||||
EC number | 1.7.3.4 | ||||||||
CAS number | 9075-43-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a hydroxylamine oxidase (EC 1.7.3.4) is an enzyme that catalyzes the chemical reaction
- hydroxylamine + O2 nitrite + H2O
Thus, the two substrates of this enzyme are hydroxylamine and O2, whereas its two products are nitrite and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with oxygen as acceptor. The systematic name of this enzyme class is hydroxylamine:oxygen oxidoreductase. Other names in common use include HAO and hydroxylamine oxidoreductase. This enzyme participates in nitrogen metabolism. It employs one cofactor, heme.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1FGJ.
References
- Hooper AB, Balny C (1982). "Reaction of oxygen with hydroxylamine oxidoreductase of Nitrosomonas: fast kinetics". FEBS Lett. 144 (2): 299–303. doi:10.1016/0014-5793(82)80658-3. PMID 7117545.
- Lipscomb JD, Hooper AB (1982). "Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 1. Electron paramagnetic resonance spectroscopy". Biochemistry. 21 (17): 3965–72. doi:10.1021/bi00260a010. PMID 6289867.
- Rees MK (1968). "Studies of the hydroxylamine metabolism of Nitrosomonas europaea. I Purification of hydroxylamine oxidase". Biochemistry. 7 (1): 353–66. doi:10.1021/bi00841a045. PMID 5758552.
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