[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/fmn-reductase-nadph-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/fmn-reductase-nadph-wikipedia\/","headline":"FMN reductase (NADPH) – Wikipedia","name":"FMN reductase (NADPH) – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Enzyme involved in redox reactions FMN reductase (NADPH) (EC 1.5.1.38, FRP, flavin reductase","datePublished":"2020-06-20","dateModified":"2020-06-20","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","url":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","height":"","width":""},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/fmn-reductase-nadph-wikipedia\/","wordCount":3174,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Enzyme involved in redox reactionsFMN 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:       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4FMNH2 + NADP+\u21cc{displaystyle rightleftharpoons } 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\u20137. doi:10.1111\/j.1432-1033.1975.tb02321.x. PMID\u00a01175652.^ Jablonski E, DeLuca M (June 1977). “Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi”. Biochemistry. 16 (13): 2932\u20136. doi:10.1021\/bi00632a020. PMID\u00a0880288.^ 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\u20138. doi:10.1021\/bi00597a018. PMID\u00a023827.^ 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\u20138. doi:10.1128\/jb.176.12.3552-3558.1994. PMC\u00a0205543. PMID\u00a08206832.^ 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\u20139. doi:10.1021\/bi961400v. PMID\u00a08885832.^ 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\u201395. doi:10.1006\/abbi.1996.9746. PMID\u00a08990272.^ Lei B, Tu SC (October 1998). “Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase”. Biochemistry. 37 (41): 14623\u20139. doi:10.1021\/bi981841+. PMID\u00a09772191.^ 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\u201346. doi:10.1074\/jbc.274.38.26639. PMID\u00a010480865.External links[edit]li{counter-increment:listitem}.mw-parser-output .hlist ol>li::before{content:\" \"counter(listitem)\"a0 \"}.mw-parser-output .hlist dd ol>li:first-child::before,.mw-parser-output .hlist dt ol>li:first-child::before,.mw-parser-output .hlist li ol>li:first-child::before{content:\" (\"counter(listitem)\"a0 \"}]]>.navbox-abovebelow,.mw-parser-output tr+tr>.navbox-group,.mw-parser-output tr+tr>.navbox-image,.mw-parser-output tr+tr>.navbox-list{border-top:2px solid #fdfdfd}.mw-parser-output .navbox-title{background-color:#ccf}.mw-parser-output .navbox-abovebelow,.mw-parser-output .navbox-group,.mw-parser-output .navbox-subgroup .navbox-title{background-color:#ddf}.mw-parser-output .navbox-subgroup .navbox-group,.mw-parser-output .navbox-subgroup .navbox-abovebelow{background-color:#e6e6ff}.mw-parser-output .navbox-even{background-color:#f7f7f7}.mw-parser-output .navbox-odd{background-color:transparent}.mw-parser-output .navbox .hlist td dl,.mw-parser-output .navbox .hlist td ol,.mw-parser-output .navbox .hlist td ul,.mw-parser-output .navbox td.hlist dl,.mw-parser-output .navbox td.hlist ol,.mw-parser-output .navbox td.hlist ul{padding:0.125em 0}.mw-parser-output .navbox .navbar{display:block;font-size:100%}.mw-parser-output .navbox-title .navbar{float:left;text-align:left;margin-right:0.5em}]]>       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Wikimedia ErrorOur servers are currently under maintenance or experiencing a technical problem.Please try again in a few\u00a0minutes.See the error message at the bottom of this page for more\u00a0information.      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