Biology:FMN reductase (NADPH)

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Short description: Enzyme involved in redox reactions
FMN reductase (NADPH)
Identifiers
EC number1.5.1.38
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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:

FMNH2 + NADP+ [math]\displaystyle{ \rightleftharpoons }[/math] FMN + NADPH + H+

The enzymes from bioluminescent bacteria contain FMN.

References

  1. "Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi". European Journal of Biochemistry 57 (2): 461–7. September 1975. doi:10.1111/j.1432-1033.1975.tb02321.x. PMID 1175652. http://www.vliz.be/imisdocs/publications/300066.pdf. 
  2. "Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi". Biochemistry 16 (13): 2932–6. June 1977. doi:10.1021/bi00632a020. PMID 880288. 
  3. "Studies of the control of luminescence in Beneckea harveyi: properties of the NADH and NADPH:FMN oxidoreductases". Biochemistry 17 (4): 672–8. February 1978. doi:10.1021/bi00597a018. PMID 23827. 
  4. "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. June 1994. doi:10.1128/jb.176.12.3552-3558.1994. PMID 8206832. 
  5. "Flavin reductase P: structure of a dimeric enzyme that reduces flavin". Biochemistry 35 (42): 13531–9. October 1996. doi:10.1021/bi961400v. PMID 8885832. 
  6. "Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium". Archives of Biochemistry and Biophysics 337 (1): 89–95. January 1997. doi:10.1006/abbi.1996.9746. PMID 8990272. 
  7. "Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase". Biochemistry 37 (41): 14623–9. October 1998. doi:10.1021/bi981841+. PMID 9772191. 
  8. "Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli". The Journal of Biological Chemistry 274 (38): 26639–46. September 1999. doi:10.1074/jbc.274.38.26639. PMID 10480865. 

External links