| Entry |
|
| Name |
renalase;
alphaNAD(P)H oxidase/anomerase (incorrect);
NAD(P)H:oxygen oxidoreductase (H2O2-forming, epimerising) (incorrect)
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| Class |
Oxidoreductases;
Acting on NADH or NADPH;
With oxygen as acceptor
 |
| Sysname |
dihydro-NAD(P):oxygen oxidoreductase (H2O2-forming)
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| Reaction(IUBMB) |
(1) 1,2-dihydro-beta-NAD(P) + H+ + O2 = beta-NAD(P)+ + H2O2 [RN: R11504];
(2) 1,6-dihydro-beta-NAD(P) + H+ + O2 = beta-NAD(P)+ + H2O2 [RN: R11505]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
Requires FAD. Renalase, previously thought to be a hormone, is a flavoprotein secreted into the blood by the kidney that oxidizes the 1,2-dihydro- and 1,6-dihydro- isomeric forms of beta-NAD(P)H back to beta-NAD(P)+. These isomeric forms, generated by nonspecific reduction of beta-NAD(P)+ or by tautomerization of beta-NAD(P)H, are potent inhibitors of primary metabolism dehydrogenases and pose a threat to normal respiration.
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| History |
EC 1.6.3.5 created 2014, modified 2015
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| Orthology |
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| Genes |
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| Reference |
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| Authors |
Xu J, Li G, Wang P, Velazquez H, Yao X, Li Y, Wu Y, Peixoto A, Crowley S, Desir GV |
| Title |
Renalase is a novel, soluble monoamine oxidase that regulates cardiac function and blood pressure. |
| Journal |
J. Clin. Invest. 115 (2005) 1275-80. |
| Sequence |
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| Reference |
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| Authors |
Beaupre BA, Hoag MR, Roman J, Forsterling FH, Moran GR |
| Title |
Metabolic function for human renalase: oxidation of isomeric forms of beta-NAD(P)H that are inhibitory to primary metabolism. |
| Journal |
Biochemistry. 54 (2015) 795-806. |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |
| LinkDB |
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