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Riboflavin reductase (NAD(P)H)

Riboflavin reductase (NAD(P)H) (EC 1.5.1.41, NAD(P)H-FMN reductase, Fre) is an enzyme with systematic name riboflavin:NAD(P)+ oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction

Riboflavin reductase (NAD(P)H)
Identifiers
EC no.1.5.1.41
Databases
IntEnzIntEnz view
BRENDABRENDA entry
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MetaCycmetabolic pathway
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NCBIproteins
reduced riboflavin + NAD(P)+ riboflavin + NAD(P)H + H+

This enzyme catalyses the reduction of soluble flavins.

The structure of the protein suggests that the enzymatic mechanism of flavin reductase is of a bisubstrate-biproduct nature3. Due to its structural features, the enzyme is not able to bind both NAD(P)H and flavin at the same time. Therefore, in the proposed mechanism the flavin reductase first binds NAD(P)H and stabilizes the release of a hydride3. Next, NAD(P)+ is released and the flavin mononucleotide binds to the enzyme. This is followed by further protonation when the hydride attacks a nitrogen atom on the flavin mononucleotide3. Finally, the reduced flavin is released from flavin reductase. If this mechanism is indeed correct, it suggests that the reduction of flavin by flavin reductase is dependent on the enzyme binding first to NAD(P)H3.

References edit

  1. ^ Fontecave M, Eliasson R, Reichard P (September 1987). "NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase". The Journal of Biological Chemistry. 262 (25): 12325–31. PMID 3305505.
  2. ^ Spyrou G, Haggård-Ljungquist E, Krook M, Jörnvall H, Nilsson E, Reichard P (June 1991). "Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme". Journal of Bacteriology. 173 (12): 3673–9. PMC 207994. PMID 2050627.
  3. ^ Ingelman M, Ramaswamy S, Nivière V, Fontecave M, Eklund H (June 1999). "Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli". Biochemistry. 38 (22): 7040–9. doi:10.1021/bi982849m. PMID 10353815.

External links edit

riboflavin, reductase, reductase, enzyme, with, systematic, name, riboflavin, oxidoreductase, this, enzyme, catalyses, following, chemical, reactionidentifiersec, 41databasesintenzintenz, viewbrendabrenda, entryexpasynicezyme, viewkeggkegg, entrymetacycmetabol. Riboflavin reductase NAD P H EC 1 5 1 41 NAD P H FMN reductase Fre is an enzyme with systematic name riboflavin NAD P oxidoreductase 1 2 3 This enzyme catalyses the following chemical reactionRiboflavin reductase NAD P H IdentifiersEC no 1 5 1 41DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins reduced riboflavin NAD P displaystyle rightleftharpoons riboflavin NAD P H H This enzyme catalyses the reduction of soluble flavins The structure of the protein suggests that the enzymatic mechanism of flavin reductase is of a bisubstrate biproduct nature3 Due to its structural features the enzyme is not able to bind both NAD P H and flavin at the same time Therefore in the proposed mechanism the flavin reductase first binds NAD P H and stabilizes the release of a hydride3 Next NAD P is released and the flavin mononucleotide binds to the enzyme This is followed by further protonation when the hydride attacks a nitrogen atom on the flavin mononucleotide3 Finally the reduced flavin is released from flavin reductase If this mechanism is indeed correct it suggests that the reduction of flavin by flavin reductase is dependent on the enzyme binding first to NAD P H3 References edit Fontecave M Eliasson R Reichard P September 1987 NAD P H flavin oxidoreductase of Escherichia coli A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase The Journal of Biological Chemistry 262 25 12325 31 PMID 3305505 Spyrou G Haggard Ljungquist E Krook M Jornvall H Nilsson E Reichard P June 1991 Characterization of the flavin reductase gene fre of Escherichia coli and construction of a plasmid for overproduction of the enzyme Journal of Bacteriology 173 12 3673 9 PMC 207994 PMID 2050627 Ingelman M Ramaswamy S Niviere V Fontecave M Eklund H June 1999 Crystal structure of NAD P H flavin oxidoreductase from Escherichia coli Biochemistry 38 22 7040 9 doi 10 1021 bi982849m PMID 10353815 External links editRiboflavin reductase NAD P H at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title Riboflavin reductase NAD P H amp oldid 1172359883, wikipedia, wiki, book, books, library,

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