Nitric oxide dioxygenase
Appearance
nitric oxide dioxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.12.17 | ||||||||
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 / QuickGO | ||||||||
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A nitric oxide dioxygenase (EC 1.14.12.17) is an enzyme that catalyzes the chemical reaction
- 2 nitric oxide + 2 O2 + NAD(P)H 2 nitrate + NAD(P)+ + H+
The 3 substrates of this enzyme are nitric oxide, O2, NADH, (or NADPH), whereas its 3 products are nitrate, NAD+, (or NADP+), and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is nitric oxide,NAD(P)H:oxygen oxidoreductase.
References
- Gardner PR (2005). "Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases". J. Inorg. Biochem. 99: 247–66. doi:10.1016/j.jinorgbio.2004.10.003. PMID 15598505.
- Gardner PR, Gardner AM, Martin LA, Salzman AL (1998). "Nitric oxide dioxygenase: an enzymic function for flavohemoglobin". Proc. Natl. Acad. Sci. U. S. A. 95: 10378–83. doi:10.1073/pnas.95.18.10378. PMID 9724711.
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: CS1 maint: multiple names: authors list (link) - Gardner PR, Costantino G, Salzman AL (1998). "Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase". J. Biol. Chem. 273: 26528–33. doi:10.1074/jbc.273.41.26528. PMID 9756889.
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: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)