Search Results

Overview

Uniprot IDP14920
Protein NameD-amino-acid oxidase
Gene NameDAO
OrganismHomo 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

10 MRVVVIGAGV 20 IGLSTALCIH 30 ERYHSVLQPL 40 DIKVYADRFT 50 PLTTTDVAAG 60 LWQPYLSDPN 70 NPQEADWSQQ 80 TFDYLLSHVH 90 SPNAENLGLF 100 LISGYNLFHE 110 AIPDPSWKDT 120 VLGFRKLTPR 130 ELDMFPDYGY 140 GWFHTSLILE 150 GKNYLQWLTE 160 RLTERGVKFF 170 QRKVESFEEV 180 AREGADVIVN 190 CTGVWAGALQ 200 RDPLLQPGRG 210 QIMKVDAPWM 220 KHFILTHDPE 230 RGIYNSPYII 240 PGTQTVTLGG 250 IFQLGNWSEL 260 NNIQDHNTIW 270 EGCCRLEPTL 280 KNARIIGERT 290 GFRPVRPQIR 300 LEREQLRTGP 310 SNTEVIHNYG 320 HGGYGLTIHW 330 GCALEAAKLF 340 GRILEEKKLS RMPPSHL

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.