Flavin reductase: Difference between revisions
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<StructureSection load='' size='350' side='right' scene='49/490853/Cv/1' caption='Human flavin reductase complex with biliverdin IX α and NADP (PDB code [[1he2]]) '> | |||
== Function == | == Function == | ||
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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. | 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 <scene name='49/490853/Cv/4'>NADP containing active site can accommodate a variety of ligands</scene> because the binding is achieved mainly via hydrophobic interactions ({{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}).<ref>PMID:11224564</ref> | |||
</StructureSection> | </StructureSection> | ||
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
{{#tree:id=OrganizedByTopic|openlevels=0| | |||
*NADPH-dependent Flavin reductase or biliverdin IX beta reductase | |||
**[[1hdo]], [[7er6]] - hFR + NADP - human<br /> | |||
**[[6opl]] – hFR (mutant) + NADP <br /> | |||
**[[1he2]] - hFR + biliverdin IX α + NADP<BR /> | |||
**[[1he3]] - hFR + mesobiliverdin IV α + NADP<BR /> | |||
**[[1he4]] - hFR + FMN + NADP<BR /> | |||
**[[1he5]] - hFR + lumichrome + NADP<BR /> | |||
**[[5ooh]] – hFR + NADP + erythrosine<br /> | |||
**[[5oog]] – hFR + NADP + phloxine + cyanosine<br /> | |||
**[[7er7]], [[7er8]], [[7er9]], [[7era]], [[7erb]], [[7erc]], [[7erd]], [[7ere]] – hFR + NADP + drug<br /> | |||
**[[3pft]] - FR (mutant) + FMN – ''Mycobacterium goodii''<br /> | |||
**[[5cho]] - FR + FAD – uncultured bacteria<br /> | |||
**[[1qfj]] – FR – ''Escherichia coli''<br /> | |||
**[[1bkj]] – VhFR + FMN – ''Vibrio harveyi''<br /> | |||
**[[2bkj]] - VhFR + NAD + FMN<br /> | |||
*NADH-dependent Flavin reductase | |||
[[ | **[[1rz0]] – GtFR + FAD – ''Geobacillus thermoglucosidasius''<br /> | ||
[[ | **[[1rz1]] - GtFR + FAD + NAD<br /> | ||
[[ | **[[5n6q]] - PpFR + FMN – ''Pseudomonas putida''<br /> | ||
[[ | **[[4uth]] - PpFR (mutant) + FMN <br /> | ||
[[ | **[[5lnj]], [[5lni]], [[4uti]], [[4utj]] - PpFR (mutant) + FMN derivative + coumarin derivative<br /> | ||
[[ | **[[2d36]] - StFR + FMN – ''Sulfurisphaera tokodaii''<br /> | ||
[[ | **[[2d37]] - StFR + FMN + NAD<br /> | ||
[[ | **[[2d38]] - StFR + FMN + NADP<br /> | ||
[[ | |||
[[ | |||
[[ | |||
}} | |||
== References == | == References == | ||
<references/> | <references/> |
Latest revision as of 12:10, 6 March 2023
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 06-March-2023
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