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   22-FEB-2012, entry version 3.
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; Scleroglossa; Serpentes; Colubroidea;
OC   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).
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:EC.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; 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; Blood coagulation; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW   Glycoprotein; Hemolysis; Oxidoreductase; 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
//