Nitric oxide dioxygenase: Difference between revisions
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NO dioxygenase belongs to the family of [[oxidoreductase]]s, more specifically those acting on paired donors, with O<sub>2</sub> as oxidant and with incorporation of two atoms of oxygen into the other donor. The systematic name of this enzyme class is '''nitric oxide,NAD(P)H:oxygen oxidoreductase'''. |
NO dioxygenase belongs to the family of [[oxidoreductase]]s, more specifically those acting on paired donors, with O<sub>2</sub> as oxidant and with incorporation of two atoms of oxygen into the other donor. The systematic name of this enzyme class is '''nitric oxide,NAD(P)H:oxygen oxidoreductase'''. |
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Enzymes catalyzing the reaction belong to the [[hemoglobin]] superfamily and include flavohemoglobin, myoglobin, neuroglobin, and cytoglobin. NO dioxygenases (NODs) are distributed to most life forms including bacteria, fungi, protists, worms, plants and animals. In fact, nitric oxide dioxygenation appears to be a primal and common function for members of the hemoglobin superfamily. NODs prevent NO toxicity and regulate NO signalling. |
Enzymes catalyzing the reaction belong to the [[hemoglobin]] superfamily and include flavohemoglobin, myoglobin, neuroglobin, and cytoglobin, although the electron donor may be ascorbate, cytochrome b<sub>5</sub> or unknown for many globins. NO dioxygenases (NODs) are distributed to most life forms including bacteria, fungi, protists, worms, plants and animals. In fact, nitric oxide dioxygenation appears to be a primal and common function for members of the hemoglobin superfamily. NODs prevent NO toxicity and regulate NO signalling. Other proteins that may act as NODs include mammalian microsomal cytochrome P450(s) and a novel O<sub>2</sub>-binding cytochrome ''b'' from ''Rhodobacter sphaeroides''. |
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==References== |
==References== |
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Revision as of 13:19, 26 November 2010
| nitric oxide dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.12.17 | ||||||||
| CAS no. | 214466-78-1 | ||||||||
| 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
- NO (nitric oxide) + O2 + NAD(P)H NO3- (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+.
NO dioxygenase belongs to the family of oxidoreductases, more specifically those acting on paired donors, with O2 as oxidant and with incorporation of two atoms of oxygen into the other donor. The systematic name of this enzyme class is nitric oxide,NAD(P)H:oxygen oxidoreductase.
Enzymes catalyzing the reaction belong to the hemoglobin superfamily and include flavohemoglobin, myoglobin, neuroglobin, and cytoglobin, although the electron donor may be ascorbate, cytochrome b5 or unknown for many globins. NO dioxygenases (NODs) are distributed to most life forms including bacteria, fungi, protists, worms, plants and animals. In fact, nitric oxide dioxygenation appears to be a primal and common function for members of the hemoglobin superfamily. NODs prevent NO toxicity and regulate NO signalling. Other proteins that may act as NODs include mammalian microsomal cytochrome P450(s) and a novel O2-binding cytochrome b from Rhodobacter sphaeroides.
References
- Gardner PR (2005). "Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases". J. Inorg. Biochem. 99 (1): 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 (18): 10378–83. doi:10.1073/pnas.95.18.10378. PMC 27902. PMID 9724711.
{{cite journal}}: 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 (41): 26528–33. doi:10.1074/jbc.273.41.26528. PMID 9756889.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)