Search Results
Overview
| Uniprot ID | P14920 |
|---|---|
| Protein Name | D-amino-acid oxidase |
| Gene Name | DAO |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 163 | GVKFFQRKVESFEEV |
| 271 | CRLEPTLKNARIIGE |
Function
Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:16616139, PubMed:17088322, PubMed:17303072, PubMed:18544534, PubMed:20368421, PubMed:20567862, PubMed:20603179, PubMed:22203986, PubMed:23219954, PubMed:23391306, PubMed:25030849, PubMed:25701391, PubMed:29274788, PubMed:29326945, PubMed:30938755, PubMed:31799256, PubMed:32730563, PubMed:33484270, PubMed:34041270, PubMed:37558109, PubMed:38035964). Required to catabolize D-amino acids synthesized endogenously, of gastrointestinal bacterial origin or obtained from the diet, and to use these as nutrients (By similarity). Regulates the level of D-amino acid neurotransmitters in the brain, such as D-serine, a co-agonist of N-methyl D-aspartate (NMDA) receptors, and may modulate synaptic transmission (PubMed:17303072). Catalyzes the first step of the racemization of D-DOPA to L-DOPA, for possible use in an alternative dopamine biosynthesis pathway (PubMed:17303072). Also catalyzes the first step of the chiral inversion of N(gamma)-nitro-D-arginine methyl ester (D-NNA) to its L-enantiomer L-NNA that acts as a nitric oxide synthase inhibitor (By similarity). The hydrogen peroxide produced in the reaction provides protection against microbial infection; it contributes to the oxidative killing activity of phagocytic leukocytes and protects against bacterial colonization of the small intestine (By similarity). Enzyme secreted into the lumen of the intestine may not be catalytically active and could instead be proteolytically cleaved into peptides with antimicrobial activity (By similarity). The hydrogen peroxide produced in the reaction may also play a role in promoting cellular senescence in response to DNA damage (PubMed:30659069). Could act as a detoxifying agent which removes D-amino acids accumulated during aging (PubMed:17303072)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005782 | peroxisomal matrix |
| Cellular Component | GO:0048786 | presynaptic active zone |
| Molecular Function | GO:0008718 | D-amino-acid dehydrogenase activity |
| Molecular Function | GO:0003884 | D-amino-acid oxidase activity |
| Molecular Function | GO:0071949 | FAD binding |
| Molecular Function | GO:0043799 | glycine oxidase activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Biological Process | GO:0055130 | D-alanine catabolic process |
| Biological Process | GO:0019478 | D-amino acid catabolic process |
| Biological Process | GO:0036088 | D-serine catabolic process |
| Biological Process | GO:0070178 | D-serine metabolic process |
| Biological Process | GO:0007586 | digestion |
| Biological Process | GO:0042416 | dopamine biosynthetic process |
| Biological Process | GO:0006562 | L-proline catabolic process |
| Biological Process | GO:0070945 | neutrophil-mediated killing of gram-negative bacterium |
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.