ID OXLA_BOTLC Reviewed; 30 AA. AC P0DI89; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 21-SEP-2011, sequence version 1. DT 19-FEB-2014, entry version 9. DE RecName: Full=L-amino-acid oxidase; DE Short=LAAO; DE Short=LAO; DE EC=1.4.3.2; DE Flags: Fragment; OS Bothrops leucurus (White-tailed jararaca) (White-tailed lancehead). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops. OX NCBI_TaxID=157295; RN [1] RP PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RP GLYCOSYLATION, AND MASS SPECTROMETRY. RC TISSUE=Venom; RX PubMed=21539897; DOI=10.1016/j.bbagen.2011.04.003; RA Naumann G.B., Silva L.F., Silva L., Faria G., Richardson M., RA Evangelista K., Kohlhoff M., Gontijo C.M., Navdaev A., RA de Rezende F.F., Eble J.A., Sanchez E.F.; RT "Cytotoxicity and inhibition of platelet aggregation caused by an l- RT amino acid oxidase from Bothrops leucurus venom."; RL Biochim. Biophys. Acta 1810:683-694(2011). CC -!- FUNCTION: Catalyzes an oxidative deamination of predominantly CC hydrophobic and aromatic L-amino acids (high activity against L- CC Met, L-Leu, L-Nle, L-Trp, L-Phe and moderate activity against L- CC Tyr), thus producing hydrogen peroxide that may contribute to the CC diverse toxic effects of this enzyme. Exhibits diverse biological CC activities, such as hemorrhage, hemolysis, edema, antibacterial CC and antiparasitic activities (By similarity). In addition, this CC protein induces apoptosis. It also interacts with endothelial CC cells, and inhibits collagen- and ADP-induced platelet CC aggregation. L-LAAO family effects on platelets are controversial, CC since it either induces aggregation or inhibits agonist-induced CC aggregation. These different effects are probably due to different CC experimental conditions. CC -!- CATALYTIC ACTIVITY: An L-amino acid + H(2)O + O(2) = a 2-oxo acid CC + NH(3) + H(2)O(2). CC -!- COFACTOR: FAD (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.5-8.8 for L-Leu; CC -!- SUBUNIT: Monomer. This is in contrast with most of its orthologs, CC that are non-covalently linked homodimers. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- PTM: N-glycosylated. CC -!- MASS SPECTROMETRY: Mass=57000; Method=MALDI; Range=1-?; CC Source=PubMed:21539897; CC -!- MISCELLANEOUS: Has parasiticidal activities against both CC trypanosomes and leishmania, as a result of enzyme-catalyzed CC hydrogen peroxide production (PubMed:21539897). CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 CC subfamily. CC -!- CAUTION: The existence of several isoforms has been reported that CC may be due to either different composition or different CC glycosylation or by the synthesis from different genes CC (PubMed:21539897). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Antibiotic; Antimicrobial; Apoptosis; Cytolysis; KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; KW Glycoprotein; Hemolysis; Hemostasis impairing toxin; Oxidoreductase; KW Platelet aggregation inhibiting toxin; Secreted; Toxin. FT CHAIN 1 >30 L-amino-acid oxidase. FT /FTId=PRO_0000412596. FT DISULFID 10 ? By similarity. FT NON_TER 30 30 SQ SEQUENCE 30 AA; 3507 MW; 37BCDB4946D486E0 CRC64; ADDRNPLEEC FRETDYEEFL EIAKNGLSTT //