A Nomenclature for the Mammalian Flavin-Containing Monooxygenase Gene Family Based on Amino Acid Sequence Identities

Lawton, Michael; Cashman, John R.; Cresteil, T.; Dolphin, Colin T.; Elfarra, Adnan A.; Hines, Ronald N.; Hodgson, Ernest; Kimura, Teruyuki; Ozols, Juris; Phillips, IR; Philpot, Richard M.; Poulsen, Lawrence L.; Rettie, Allan E.; Shephard, Elizabeth A.; Williams, David E.; Ziegler, Daniel M.

doi:10.1006/abbi.1994.1035

Cited by 181 publications

(96 citation statements)

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“…Similar size for FMOgs-ox proteins have been reported from other species such as Arabidopsis, human, yeast, and rice 4,13,[35][36][37] . In silico analysis of conserved sequences for FMO protein attributes such as FMO identifying motif (FxGxxxHxxxY/F), FAD-and NADPHbinding motif (GxGxxG) are evident to exists in RsFMOgs-ox1.…”

Section: Discussionsupporting

confidence: 81%

Isolation and expression of FMOgs-ox1 from Korean radish

Sugiharti¹,

Su’udi²,

Lim³

et al. 2014

ScienceAsia

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Flavin monooxygenase (FMO) is one of the most important enzymes involved in glucosinolate biosynthesis. In this study, the full length of FMO gene (RsFMOgs-ox1) encoding a putative FMO protein composed of 450 amino acids was successfully cloned using the RACE-PCR method. The amino acid sequence of RsFMOgs-ox1 has high similarities of 92% and 83% with BrFMOgs-ox1 and AtFMOgs-ox1,2,3, respectively, and the gene structure of FMOgs-ox1 is similar to its plant homologues. Quantitative (qPCR) analysis revealed that RsFMOgs-ox1 was highly expressed during early seedling development. In mature radish, the highest expression was observed in the leaves, while the lowest transcript was evident in the root. The expression of RsFMOgs-ox1 was also regulated by wounding, notably 1 day after treatment. Subcellular localization in Arabidopsis showed that RsFMOgs-ox1 was localized in the cytoplasm and nuclei. This study allows us to understand something about RsFMOgs-ox1 function in glucosinolate biosynthesis.

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Section: Discussionsupporting

confidence: 81%

Isolation and expression of FMOgs-ox1 from Korean radish

Sugiharti¹,

Su’udi²,

Lim³

et al. 2014

ScienceAsia

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“…We now know that humans possess five functional FMO genes (FMO1 to FMO5) [11][12][13]. FMO1 to FMO4 are clustered on chromosome 1 at q24.3 [13], along with a pseudogene, FMO6P [13,14].…”

Section: The Fmo Family Of Humansmentioning

confidence: 99%

Flavin-containing monooxygenases: mutations, disease and drug response

Phillips

Shephard

2008

Trends in Pharmacological Sciences

118

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“…Since those early studies, FMOs have been purified and/or cloned from multiple sources (Table 1). Until recently, it was thought that only 5 genes were expressed in mammals Lawton et al, 1994;Cashman, 1995;Phillips et al, 1995). A sixth human gene, FMO6, identified by the Sanger Center chromosome 1 sequencing project, was demonstrated to be a psuedogene .…”

Section: Introductionmentioning

confidence: 99%

Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism

Krueger

Williams

2005

Pharmacology & Therapeutics

515

444

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Flavin-containing monooxygenase (FMO) oxygenates drugs and xenobiotics containing a "softnucleophile", usually nitrogen or sulfur. FMO, like cytochrome P450 (CYP), is a monooxygenase, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate. FMO and CYP also exhibit similar tissue and cellular location, molecular weight, substrate specificity, and exist as multiple enzymes under developmental control. The human FMO functional gene family is much smaller (5 families each with a single member) than CYP. FMO does not require a reductase to transfer electrons from NADPH and the catalytic cycle of the 2 monooxygenases is strikingly different. Another distinction is the lack of induction of FMOs by xenobiotics.In general, CYP is the major contributor to oxidative xenobiotic metabolism. However, FMO activity may be of significance in a number of cases and should not be overlooked. FMO and CYP have overlapping substrate specificities, but often yield distinct metabolites with potentially significant toxicological/pharmacological consequences.The physiological function(s) of FMO are poorly understood. Three of the 5 expressed human FMO genes, FMO1, FMO2 and FMO3, exhibit genetic polymorphisms. The most studied of these is FMO3 (adult human liver) in which mutant alleles contribute to the disease known as trimethylaminuria. The consequences of these FMO genetic polymorphisms in drug metabolism and human health are areas of research requiring further exploration.

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A Nomenclature for the Mammalian Flavin-Containing Monooxygenase Gene Family Based on Amino Acid Sequence Identities

Cited by 181 publications

References 0 publications

Isolation and expression of FMOgs-ox1 from Korean radish

Isolation and expression of FMOgs-ox1 from Korean radish

Flavin-containing monooxygenases: mutations, disease and drug response

Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism

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