FMN reductase

FMN還元酵素、FMNレダクターゼ

WordNet

1. an enzyme that catalyses the biochemical reduction of some specified substance
2. the 6th letter of the Roman alphabet (同)f

PrepTutorEJDIC

1. frequency modulation 周波数変調

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/08/17 15:29:26」(JST)

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FMN reductase
Identifiers
EC number	1.5.1.29
CAS number	64295-83-6
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, an FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction

FMNH₂ + NAD(P)+ FMN + NAD(P)H + H⁺

The 3 substrates of this enzyme are FMNH2, NAD⁺, and NADP⁺, whereas its 4 products are FMN, NADH, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is FMNH2:NAD(P)+ oxidoreductase. Other names in common use include NAD(P)H-FMN reductase, NAD(P)H-dependent FMN reductase, NAD(P)H:FMN oxidoreductase, NAD(P)H:flavin oxidoreductase, NAD(P)H2 dehydrogenase (FMN), NAD(P)H2:FMN oxidoreductase, SsuE, riboflavin mononucleotide reductase, flavine mononucleotide reductase, riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide, (phosphate)) reductase, flavin mononucleotide reductase, and riboflavine mononucleotide reductase.

References

• Duane W, Hastings JW (1975). "Flavin mononucleotide reductase of luminous bacteria". Mol. Cell. Biochem. 6 (1): 53–64. doi:10.1007/BF01731866. PMID 47604. 
• Fisher J, Spencer R, Walsh C (1976). "Enzyme-catalyzed redox reactions with the flavin analogues 5-deazariboflavin, 5-deazariboflavin 5'-phosphte, and 5-deazariboflavin 5'-diphosphate, 5' leads to 5'-adenosine ester". Biochemistry. 15 (5): 1054–64. doi:10.1021/bi00650a016. PMID 3207. 
• Tu SC, Becvar JE, Hastings JW (1979). "Kinetic studies on the mechanism of bacterial NAD(P)H:flavin oxidoreductase". Arch. Biochem. Biophys. 193 (1): 110–6. doi:10.1016/0003-9861(79)90013-4. PMID 222213. 
• Liu M, Lei B, Ding Q, Lee JC, Tu SC (1997). "Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium". Arch. Biochem. Biophys. 337 (1): 89–95. doi:10.1006/abbi.1996.9746. PMID 8990272. 
• Lei B, Tu SC (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. 
• Tang CK, Jeffers CE, Nichols JC, Tu SC (2001). "Flavin specificity and subunit interaction of Vibrio fischeri general NAD(P)H-flavin oxidoreductase FRG/FRase I". Arch. Biochem. Biophys. 392 (1): 110–6. doi:10.1006/abbi.2001.2396. PMID 11469801. 
• Ingelman M, Ramaswamy S, Niviere V, Fontecave M, Eklund H (1999). "Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli". Biochemistry. 38 (22): 7040–9. doi:10.1021/bi982849m. PMID 10353815. 
• Eichhorn E, van der Ploeg JR, Leisinger T (1999). "Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli". J. Biol. Chem. 274 (38): 26639–46. doi:10.1074/jbc.274.38.26639. PMID 10480865. 

UpToDate Contents

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English Journal

• Endothelial nitric oxide synthase is regulated by ERK phosphorylation at S602.

• Salerno JC, Ghosh DK, Razdan R, Helms KA, Brown CC, McMurry JL, Rye EA, Chrestensen CA.
• Bioscience reports.Biosci Rep.2014 Jul 7. [Epub ahead of print]
• Endothelial nitric oxide synthase contains a MAP kinase binding site associated with a major eNOS control element. Purified ERK phosphorylates eNOS with a stoichiometry of 2-3 phosphates per eNOS monomer. Phosphorylation decreases NO synthesis and cytochrome c reductase activity. Three sites of phos
• PMID 25000310

• Localization-controlled specificity of FAD:threonine flavin transferases in Klebsiella pneumoniae and its implications for the mechanism of Na(+)-translocating NADH:quinone oxidoreductase.

• Bertsova YV1, Kostyrko VA1, Baykov AA1, Bogachev AV2.
• Biochimica et biophysica acta.Biochim Biophys Acta.2014 Jul;1837(7):1122-9. doi: 10.1016/j.bbabio.2013.12.006. Epub 2013 Dec 20.
• The Klebsiella pneumoniae genome contains genes for two putative flavin transferase enzymes (ApbE1 and ApbE2) that add FMN to protein Thr residues. ApbE1, but not ApbE2, has a periplasm-addressing signal sequence. The genome also contains genes for three target proteins with the Dxx(s/t)gAT flavinyl
• PMID 24361839

• Architecture of the Nitric-oxide Synthase Holoenzyme Reveals Large Conformational Changes and a Calmodulin-driven Release of the FMN Domain.

• Yokom AL1, Morishima Y2, Lau M2, Su M3, Glukhova A4, Osawa Y2, Southworth DR5.
• The Journal of biological chemistry.J Biol Chem.2014 Jun 13;289(24):16855-16865. Epub 2014 Apr 15.
• Nitric-oxide synthase (NOS) is required in mammals to generate NO for regulating blood pressure, synaptic response, and immune defense. NOS is a large homodimer with well characterized reductase and oxygenase domains that coordinate a multistep, interdomain electron transfer mechanism to oxidize l-a
• PMID 24737326

Japanese Journal

• Purification and Characterization of Fe(III)-EDTA Reductase from Bacillus sp. B-3

• SHINAGAWA Emiko
• Bioscience, biotechnology, and biochemistry 75(10), 2063-2065, 2011-10-23
• … Fe(III)-EDTA reductase was purified from <I>Bacillus</I> … The purified enzyme showed a single protein band corresponding to a molecular mass of 19 kDa on SDS–PAGE, and had FMN as cofactor. …
• NAID 10029873377

• Characterization of a flavin reductase from a thermophilic dibenzothiophene-desulfurizing bacterium, Bacillus subtilis WU-S2B(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

• Takahashi Shusuke,Furuya Toshiki,Ishii Yoshitaka,Kino Kuniki,Kirimura Kohtaro
• Journal of bioscience and bioengineering 107(1), 38-41, 2009-01
• … Bacillus subtilis WU-S2B is a thermophilic dibenzothiophene (DBT)-desulfurizing bacterium and produces a flavin reductase (Frb) that couples with DBT and DBT sulfone monooxygenases. … Frb contained FMN and exhibited both flavin reductase and nitroreductase activities. …
• NAID 110007042028

Related Links

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• FMN reductase - Freebase

In enzymology, an FMN reductase is an enzyme that catalyzes the chemical reaction+ The 3 substrates of this enzyme are FMNH2, NAD+, and NADP+, whereas its 4 products are FMN, NADH, NADPH, and H+. This enzyme ...

Related Pictures

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★リンクテーブル★

リンク元	「FMN還元酵素」「FMNレダクターゼ」
関連記事	「FM」「reductase」「FMN」「F」

「FMN還元酵素」

　　[★]

英

FMN reductase

関

FMNレダクターゼ

「FMNレダクターゼ」

　　[★]

英

FMN reductase

関

FMN還元酵素

「FM」

　　[★]

• フィブリンモノマー fibrin monomer
• 線維筋痛症 fibromyalgia
• 胎動 fetal movement
• 劇症型心筋炎 fulminant myocarditis
• 周波数変調 frequency modulation

• FBM？ fetal breathing movement？

　

「reductase」

　　[★]

• n.

(酵素)還元酵素、レダクターゼ、リダクターゼ

関

dehydrogenase、oxidase、oxidoreductase、reducing enzyme

　

「FMN」

　　[★] フラビンモノヌクレオチド flavin adenine dinucleotide

「F」

　　[★] フェニルアラニン phenylalanine