Search Results
Overview
| Uniprot ID | P49326 |
|---|---|
| Protein Name | Flavin-containing monooxygenase 5 |
| Gene Name | FMO5 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 168 | FPGIEKFKGQYFHSR |
| 186 | NPEGFTGKRVIIIGI |
| 255 | CGQSLANKYLEKKIN |
| 273 | DHEMFGLKPKHRALS |
| 275 | EMFGLKPKHRALSQH |
| 480 | YRVQGPGKWDGARKA |
| 486 | GKWDGARKAILTTDD |
| 57 | EGRASIYKSVIINTS |
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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Molecular Function | GO:0050660 | flavin adenine dinucleotide binding |
| Molecular Function | GO:0004497 | monooxygenase activity |
| Molecular Function | GO:0004499 | N,N-dimethylaniline monooxygenase activity |
| Molecular Function | GO:0016174 | NAD(P)H oxidase H2O2-forming activity |
| Molecular Function | GO:0050661 | NADP binding |
| Biological Process | GO:0006629 | lipid metabolic process |
| Biological Process | GO:0090181 | regulation of cholesterol metabolic process |
| Biological Process | GO:0006805 | xenobiotic metabolic process |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.