Flavin reductase

From Wikipedia, the free encyclopedia

In enzymology, a flavin reductase (EC 1.5.1.30) is an enzyme that catalyzes the chemical reaction

reduced riboflavin + NADP⁺ $\rightleftharpoons$ riboflavin + NADPH + H⁺

Thus, the two substrates of this enzyme are reduced riboflavin and NADP⁺, whereas its 3 products are riboflavin, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD⁺ or NADP⁺ as acceptor. The systematic name of this enzyme class is reduced-riboflavin:NADP+ oxidoreductase. Other names in common use include NADPH:flavin oxidoreductase, riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide, phosphate) reductase, flavin mononucleotide reductase, flavine mononucleotide reductase, FMN reductase (NADPH), NADPH-dependent FMN reductase, NADPH-flavin reductase, NADPH-FMN reductase, NADPH-specific FMN reductase, riboflavin mononucleotide reductase, riboflavine mononucleotide reductase, NADPH2 dehydrogenase (flavin), and NADPH2:riboflavin oxidoreductase.

[edit] References

IUBMB entry for 1.5.1.30
BRENDA references for 1.5.1.30 (Recommended.)
PubMed references for 1.5.1.30
PubMed Central references for 1.5.1.30
Google Scholar references for 1.5.1.30
Lo H, Reeves RE (1980). "Purification and properties of NADPH:flavin oxidoreductase from Entamoeba histolytica". Mol. Biochem. Parasitol. 2: 23–30. doi:10.1016/0166-6851(80)90045-6. PMID 6258069.
Yubisui T, Tamura M, Takeshita M (1987). "Characterization of a second form of NADPH-flavin reductase purified from human erythrocytes". Biochem. Int. 15: 1–8. PMID 3453680.