Recombinant Human FMO5 Protein

Tag: C-His. Modification: unmodified. Start Site: Gly271. End Site: Ala460. Coverage: 0.38. Isoelectric Point: 6.5. Core Sequence: GLKPKHRALS QHPTLNDDLP NRIISGLVKV KGNVKEFTET AAIFEDGSRE DDIDAVIFAT GYSFDFPFLE DSVKVVKNKI SLYKKVFPPN LERPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKTLP SQSEMMAEIS KAQEEIDKRY VESQRHTIQG DYIDTMEELA DLVGVRPNLL SLAFTDPKLA. Homologies: Highest protein sequence identity to the following orthologs: Mouse - 90%, Rat - 91%, Pig - 91%, Cynomolgus monkey - 97%, Protein Function: Acts as a Baeyer-Villiger monooxygenase on a broad range of substrates. Catalyzes the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters (PubMed:20947616, PubMed:26771671, PubMed:28783300). Active on diverse carbonyl compounds, whereas soft nucleophiles are mostly non- or poorly reactive (PubMed:26771671, PubMed:7872795). In contrast with other forms of FMO it is non- or poorly active on 'classical' substrates such as drugs, pesticides, and dietary components containing soft nucleophilic heteroatoms (Probable) (PubMed:7872795). Able to oxidize drug molecules bearing a carbonyl group on an aliphatic chain, such as nabumetone and pentoxifylline (PubMed:28783300). Also, in the absence of substrates, shows slow but yet significant NADPH oxidase activity (PubMed:26771671). Acts as a positive modulator of cholesterol biosynthesis as well as glucose homeostasis, promoting metabolic aging via pleiotropic effects (By similarity) [The Uniprot Consortium]