Flavin reductase
FunctionFlavin reductase (FR) catalyzes the NADPH-dependent reduction of a variety of flavins such as riboflavin, FAD, FMN, biliverdin, methemoglobin and pyrroloquinoline quinone. FR converts reduced riboflavin to riboflavin and bilirubin to biliverdin. FR is involved in heme catabolism[1] . RelevanceFR catalytic reaction is the basis of the therapeutic use of methylene blue or riboflavin in the treatment of methemoglobinemia. Bacterial FR are used to sensitize tumors to drugs. Structural insightsThe because the binding is achieved mainly via hydrophobic interactions (Hydrophobic, Polar).[2] |
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3D structures of flavin reductase3D structures of flavin reductase
Updated on 26-January-2016
1qfj – FR – Escherichia coli
1bkj – VhFR + FMN – Vibrio harveyi
2bkj - VhFR + NAD + FMN
1hdo - hFR + NADP - human
1he2 - hFR + biliverdin IX α + NADP
1he3 - hFR + mesobiliverdin IV α + NADP
1he4 - hFR + FMN + NADP
1he5 - hFR + lumichrome + NADP
1rz0 – GtFR + FAD – Geobacillus thermoglucosidasius
1rz1 - GtFR + FAD + NAD
3pft - FR (mutant) + FMN – Mycobacterium goodii
ReferencesReferences
- ↑ Yubisui T, Takeshita M, Yoneyama Y. Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. J Biochem. 1980 Jun;87(6):1715-20. PMID:7400118
- ↑ Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M. Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme. Nat Struct Biol. 2001 Mar;8(3):215-20. PMID:11224564 doi:10.1038/84948