Flavin-containing monooxygenase
http://dbpedia.org/resource/Flavin-containing_monooxygenase an entity of type: Thing
The flavin-containing monooxygenase (FMO) protein family specializes in the oxidation of xeno-substrates in order to facilitate the excretion of these compounds from living organisms. These enzymes can oxidize a wide array of heteroatoms, particularly soft nucleophiles, such as amines, sulfides, and phosphites. This reaction requires an oxygen, an NADPH cofactor, and an FAD prosthetic group. FMOs share several structural features, such as a NADPH binding domain, FAD binding domain, and a conserved arginine residue present in the active site. Recently, FMO enzymes have received a great deal of attention from the pharmaceutical industry both as a drug target for various diseases and as a means to metabolize pro-drug compounds into active pharmaceuticals. These monooxygenases are often miscla
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フラビン含有モノオキシゲナーゼ(flavin-containing monooxygenase)は、メタン代謝酵素の一つで、次の化学反応を触媒する酸化還元酵素である。 N,N-ジメチルアニリン + NADPH + H+ + O2 N,N-ジメチルアニリン N-オキシド + NADP+ + H2O 反応式の通り、この酵素の基質はN,N-ジメチルアニリンとNADPHとH+とO2、生成物はとNADP+とH2Oである。補酵素としてFADとフラビンを用いる。
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La monoossigenasi contenente flavina è un enzima appartenente alla classe delle ossidoreduttasi, che catalizza la seguente reazione: N,N-dimetilanilina + NADPH + H+ + O2 ⇄ N,N-dimetilanilina N-ossido + NADP+ + H2O L'enzima è una flavoproteina che presenta un ampio spettro di specificità. Agisce infatti su substrati diversissimi come idrazine, fosfine, composti contenenti boro, solfuri, composti del selenio, dello iodio ed ammine primarie, secondarie e terziarie.
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Flavin-containing monooxygenase
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Monoossigenasi contenente flavina
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フラビン含有モノオキシゲナーゼ
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Flavin-containing monooxygenase
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Flavin-containing monooxygenase FMO
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Ribbon diagram of yeast FMO .
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IPR000960
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PF00743
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Flavin_mOase
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The flavin-containing monooxygenase (FMO) protein family specializes in the oxidation of xeno-substrates in order to facilitate the excretion of these compounds from living organisms. These enzymes can oxidize a wide array of heteroatoms, particularly soft nucleophiles, such as amines, sulfides, and phosphites. This reaction requires an oxygen, an NADPH cofactor, and an FAD prosthetic group. FMOs share several structural features, such as a NADPH binding domain, FAD binding domain, and a conserved arginine residue present in the active site. Recently, FMO enzymes have received a great deal of attention from the pharmaceutical industry both as a drug target for various diseases and as a means to metabolize pro-drug compounds into active pharmaceuticals. These monooxygenases are often misclassified because they share activity profiles similar to those of cytochrome P450 (CYP450), which is the major contributor to oxidative xenobiotic metabolism. However, a key difference between the two enzymes lies in how they proceed to oxidize their respective substrates; CYP enzymes make use of an oxygenated heme prosthetic group, while the FMO family utilizes FAD to oxidize its substrates.
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フラビン含有モノオキシゲナーゼ(flavin-containing monooxygenase)は、メタン代謝酵素の一つで、次の化学反応を触媒する酸化還元酵素である。 N,N-ジメチルアニリン + NADPH + H+ + O2 N,N-ジメチルアニリン N-オキシド + NADP+ + H2O 反応式の通り、この酵素の基質はN,N-ジメチルアニリンとNADPHとH+とO2、生成物はとNADP+とH2Oである。補酵素としてFADとフラビンを用いる。 組織名はN,N-dimethylaniline,NADPH:oxygen oxidoreductase (N-oxide-forming)で、別名にdimethylaniline oxidase、dimethylaniline N-oxidase、FAD-containing monooxygenase、N,N-dimethylaniline monooxygenase、DMA oxidase、flavin mixed function oxidase、Ziegler's enzyme、mixed-function amine oxidase、FMO、FMO-I、FMO-II、FMO1、FMO2、FMO3、FMO4、FMO5、flavin monooxygenase、methylphenyltetrahydropyridine N-monooxygenase、1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine:oxygen N-oxidoreductase、dimethylaniline monooxygenase (N-oxide-forming)がある。
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La monoossigenasi contenente flavina è un enzima appartenente alla classe delle ossidoreduttasi, che catalizza la seguente reazione: N,N-dimetilanilina + NADPH + H+ + O2 ⇄ N,N-dimetilanilina N-ossido + NADP+ + H2O L'enzima è una flavoproteina che presenta un ampio spettro di specificità. Agisce infatti su substrati diversissimi come idrazine, fosfine, composti contenenti boro, solfuri, composti del selenio, dello iodio ed ammine primarie, secondarie e terziarie. L'enzima è differente dalle altre monoossigenasi perché forma un intermedio idroperossido flavinico relativamente stabile. Questo enzima microsomiale converte generalmente composti chimici contenenti regioni nucleofile in sostanze innocue, pronte per essere escrete. Ad esempio, la N-ossigenazione è ampiamente responsabile della detossificazione della neurotossina dopaminergica 1-metile-4-fenile-1,2,3,6-tetraidropiridina (MPTP). Individui con una carenza genetica di questo enzima possiedono la sindrome "dell'odore di pesce": il mancato metabolismo della trimetilamina, dal caratteristico odore, ne causa una sua escrezione in urine, sudore e aria espirata.
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1.14.13.8