FMO2 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
Aliases | FMO2, FMO1B1, flavin containing monooxygenase 2, flavin containing dimethylaniline monoxygenase 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 603955; MGI: 1916776; HomoloGene: 86882; GeneCards: FMO2; OMA:FMO2 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Dimethylaniline monooxygenase [N-oxide-forming] 2 is an enzyme that in humans is encoded by the FMO2 gene.[5][6][7]
The flavin-containing monooxygenases are NADPH-dependent enzymes that catalyze the oxidation of many drugs and xenobiotics. In most mammals, there is a flavin-containing monooxygenase that catalyzes the N-oxidation of some primary alkylamines through an N-hydroxylamine intermediate. However, in humans, this enzyme is truncated and is probably rapidly degraded. The protein encoded by this gene represents the truncated form and apparently has no catalytic activity. A functional allele found in African Americans has been reported, but no sequence evidence has been deposited to support the finding. This gene is found in a cluster with the FMO1, FMO3, and FMO4 genes on chromosome 1.[7]
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1.14.11: 2-oxoglutarate |
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1.14.13: NADHorNADPH |
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1.14.14: reduced flavinorflavoprotein |
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1.14.15: reduced iron–sulfur protein |
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1.14.16: reduced pteridine (BH4 dependent) |
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1.14.17: reduced ascorbate |
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1.14.18-19: other |
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1.14.99 - miscellaneous |
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