Flavin reductase

From Proteopedia

Revision as of 09:13, 18 May 2017

spinqualitylabelsall models Human flavin reductase complex with biliverdin IX α and NADP (PDB code 1he2) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Flavin 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] . Relevance FR 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 insights The because the binding is achieved mainly via hydrophobic interactions (Hydrophobic, Polar).[2]

3D structures of flavin reductase

Updated on 18-May-2017

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
5cho - FR + FAD – uncultured bacteria

References

1. ↑ 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
2. ↑ 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