Regular ArticleCharacterization of Flavin-Containing Monooxygenase-5 (FMO5) Cloned from Human and Guinea-Pig: Evidence That the Unique Catalytic Properties of FMO5 Are Not Confined to the Rabbit Ortholog
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Prenatal diagnosis of a familial 1q21.1-q21.2 microdeletion in a fetus with polydactyly of left foot on prenatal ultrasound
2018, Taiwanese Journal of Obstetrics and GynecologyCitation Excerpt :PRKAB2 is expressed in skeletal and cardiac muscles [23]. FMO5 (OMIM 603957) encodes flavin-containing monooxygenase 5, which catalyzes the nucleophilic nitrogen, sulfur and phosphorus atoms and is expressed in human liver [25,26]. CHD1L (OMIM 613039) encodes chromodomain helicase DNA-binding protein 1-like, which plays a role in chromatin relaxation following DNA damage [27].
Monoamine Oxidases and Flavin-Containing Monooxygenases
2018, Comprehensive Toxicology: Third EditionThe phenotype of a knockout mouse identifies flavin-containing monooxygenase 5 (FMO5) as a regulator of metabolic ageing
2015, Biochemical PharmacologyCitation Excerpt :FMO5 displays few characteristics of an enzyme involved in the detoxification of small foreign chemicals, with little or no activity towards classic FMO substrates, such as methimazole [12], trimethylamine [13] and benzydamine [14]. Knowledge of its substrates is limited [2,15,16]: it catalyzes the N-oxygenation of short-chain aliphatic primary amines such as N-octylamine [12] and the S-oxygenation of S-methyl-esonarimod, an active metabolite of the anti-rheumatic esonarimod [15,17]. The ability of FMO5 to catalyze a Baeyer–Villiger oxidation reaction was revealed in a study of an anti-cancer therapeutic [18].
PH dependence on functional activity of human and mouse flavin-containing monooxygenase 5
2012, Biochemical PharmacologyCitation Excerpt :This is primarily due to a paucity of selective substrates. With typical FMO substrates such as methimazole or trimethylamine FMO5 does not show any functional activity [8], whereas it oxygenates long-chain phenothiazene analogs (i.e., 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene (8-DPT)) [8], n-octylamine [9,10], and S-methyl-esonarimod and its methoxy-analog [8,11]. A unique feature of mouse FMO5 (mFMO) is that when compared to the pH dependence of three other functional mFMOs (i.e., mFMO1, mFMO3, and mFMO4) and human FMO5 (hFMO5), it was found that the pH profile of mFMO5 differed significantly from that of all other FMO forms examined in the study [8].
Monoamine Oxidases and Flavin-Containing Monooxygenases
2010, Comprehensive Toxicology, Second EditionPhase I biotransformation reactions-flavin monooxygenase
2007, xPharm: The Comprehensive Pharmacology Reference