FMN reductase (NADPH) (EC 1.5.1.38, FRP, flavin reductase P, SsuE) is an enzyme with systematic name FMNH2:NADP+ oxidoreductase.[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction:
| FMN reductase (NADPH) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.1.38 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- FMNH2 + NADP+ FMN + NADPH + H+
The enzymes from bioluminescent bacteria contain FMN.
References edit
- ^ Gerlo E, Charlier J (September 1975). "Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi" (PDF). European Journal of Biochemistry. 57 (2): 461–7. doi:10.1111/j.1432-1033.1975.tb02321.x. PMID 1175652.
- ^ Jablonski E, DeLuca M (June 1977). "Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi". Biochemistry. 16 (13): 2932–6. doi:10.1021/bi00632a020. PMID 880288.
- ^ Jablonski E, DeLuca M (February 1978). "Studies of the control of luminescence in Beneckea harveyi: properties of the NADH and NADPH:FMN oxidoreductases". Biochemistry. 17 (4): 672–8. doi:10.1021/bi00597a018. PMID 23827.
- ^ Lei B, Liu M, Huang S, Tu SC (June 1994). "Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme". Journal of Bacteriology. 176 (12): 3552–8. doi:10.1128/jb.176.12.3552-3558.1994. PMC 205543. PMID 8206832.
- ^ Tanner JJ, Lei B, Tu SC, Krause KL (October 1996). "Flavin reductase P: structure of a dimeric enzyme that reduces flavin". Biochemistry. 35 (42): 13531–9. doi:10.1021/bi961400v. PMID 8885832.
- ^ Liu M, Lei B, Ding Q, Lee JC, Tu SC (January 1997). "Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium". Archives of Biochemistry and Biophysics. 337 (1): 89–95. doi:10.1006/abbi.1996.9746. PMID 8990272.
- ^ Lei B, Tu SC (October 1998). "Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase". Biochemistry. 37 (41): 14623–9. doi:10.1021/bi981841+. PMID 9772191.
- ^ Eichhorn E, van der Ploeg JR, Leisinger T (September 1999). "Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli". The Journal of Biological Chemistry. 274 (38): 26639–46. doi:10.1074/jbc.274.38.26639. PMID 10480865.
External links edit
- FMN+reductase+(NADPH) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
