FMN reductase (NADPH) - Misplaced Pages

FMN reductase (NADPH) (EC 1.5.1.38, FRP, flavin reductase P, SsuE) is an enzyme with systematic name FMNH₂:NADP oxidoreductase. This enzyme catalyses the following chemical reaction:

FMNH2 + NADP

\rightleftharpoons

FMN + NADPH + H

The enzymes from bioluminescent bacteria contain FMN.

References

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

FMN+reductase+(NADPH) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Oxidoreductases: CH-NH (EC 1.5)
1.5.1: NAD or NADP acceptor	Dihydrofolate reductase Saccharopine dehydrogenase Methylenetetrahydrofolate reductase
1.5.3: oxygen acceptor	Dihydrobenzophenanthridine oxidase Sarcosine oxidase Proline oxidase
1.5.5: quinone acceptor	Electron-transferring-flavoprotein dehydrogenase
1.5.99	Sarcosine dehydrogenase Cytokinin dehydrogenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 1.5.1