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FMO5

Protein-coding gene in humans From Wikipedia, the free encyclopedia

Dimethylaniline monooxygenase [N-oxide-forming] 5 is an enzyme in humans encoded by the FMO5 gene.[5][6][7]

AliasesFMO5, flavin containing monooxygenase 5, flavin containing dimethylaniline monoxygenase 5, hBVMO1
External IDsOMIM: 603957; MGI: 1310004; GeneCards: FMO5
End147,243,050 bp[1]
Quick facts Identifiers, Aliases ...
FMO5
Identifiers
AliasesFMO5, flavin containing monooxygenase 5, flavin containing dimethylaniline monoxygenase 5, hBVMO1
External IDsOMIM: 603957; MGI: 1310004; GeneCards: FMO5
Enzyme activity
EC #BRENDAExPASyKEGGMetaCyc
1.6.3.1↗↗↗↗
1.14.13.8↗↗↗↗
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001144829
NM_001144830
NM_001461

NM_001161763
NM_001161765
NM_010232
NM_001355119

RefSeq (protein)

NP_001138301
NP_001138302
NP_001452

NP_001155235
NP_001155237
NP_034362
NP_001342048

Location (UCSC)Chr 1: 147.18 – 147.24 MbChr 3: 97.54 – 97.56 Mb
PubMed search[3][4]
Wikidata
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Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in man resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome Trimethylaminuria. Three forms of the enzyme, FMO1 found in fetal liver, FMO2 found in adult liver, and FMO3 are encoded by genes clustered in the 1q23-q25 region. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in drugs, pesticides, and xenobiotics.[7]

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