EC 1.6.3.5 - Renalase

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IntEnz Enzyme Nomenclature
EC 1.6.3.5

Names

Accepted name:
renalase
Other names:
αNAD(P)H oxidase/anomerase [incorrect]
α-NAD(P)H oxidase/anomerase [incorrect]
NAD(P)H:oxygen oxidoreductase (H2O2-forming, epimerising) [incorrect]
Systematic name:
dihydro-NAD(P):oxygen oxidoreductase (H2O2-forming)

Reactions

Cofactor

Comments:

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 β-NAD(P)H back to β-NAD(P)+. These isomeric forms, generated by nonspecific reduction of β-NAD(P)+ or by tautomerization of β-NAD(P)H, are potent inhibitors of primary metabolism dehydrogenases and pose a threat to normal respiration.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Xu, J., Li, G., Wang, P., Velazquez, H., Yao, X., Li, Y., Wu, Y., Peixoto, A., Crowley, S., Desir, G. V.
    Renalase is a novel, soluble monoamine oxidase that regulates cardiac function and blood pressure.
    J. Clin. Invest. 115: 1275-1280 (2005). [PMID: 15841207]
  2. Beaupre, B. A., Hoag, M. R., Roman, J., Forsterling, F. H., Moran, G. R.
    Metabolic function for human renalase: oxidation of isomeric forms of beta-NAD(P)H that are inhibitory to primary metabolism.
    Biochemistry 54: 795-806 (2015). [PMID: 25531177]

[EC 1.6.3.5 created 2014, modified 2015]