ID   OXLA_CRODC              Reviewed;          61 AA.
AC   P0C2D2;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 16.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LAO;
DE            Short=Casca LAO;
DE            EC=1.4.3.2;
DE   Flags: Fragment;
OS   Crotalus durissus cascavella (Northeastern Brazilian rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=184540;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=16307769; DOI=10.1016/j.toxicon.2005.09.008;
RA   Toyama M.H., Toyama Dde O., Passero L.F., Laurenti M.D., Corbett C.E.,
RA   Tomokane T.Y., Fonseca F.V., Antunes E., Joazeiro P.P., Beriam L.O.,
RA   Martins M.A., Monteiro H.S., Fonteles M.C.;
RT   "Isolation of a new L-amino acid oxidase from Crotalus durissus
RT   cascavella venom.";
RL   Toxicon 47:47-57(2006).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids. Induces a dose-dependent
CC       platelet aggregation. Has an ability to induce apoptosis. Has an
CC       antibacterial activity against both Gram-negative and Gram-
CC       positive bacteria. Has high antileishmanic activity against the
CC       promastigote of Leishmania amazonensis in vitro. May have an
CC       ability to induce hemorrhage.
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.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=46.7 uM for L-Leu;
CC       pH dependence:
CC         Optimum pH is 6.5;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily.
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DR   SMR; P0C2D2; 3-61.
DR   HOVERGEN; P0C2D2; -.
DR   BRENDA; 1.4.3.2; 274610.
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:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   Pfam; PF01266; DAO; 1.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Blood coagulation;
KW   Direct protein sequencing; FAD; Flavoprotein; Glycoprotein;
KW   Oxidoreductase; Secreted; Toxin.
FT   CHAIN         1    >61       L-amino-acid oxidase.
FT                                /FTId=PRO_0000273567.
FT   NON_TER      61     61
SQ   SEQUENCE   61 AA;  6561 MW;  9D7F04E64267A122 CRC64;
     ADDRNPLEQC FRETDYEEFL EIARNNLKAT SNPKHVVIVG AGMAGLSAAY VLSGGGHQVT
     V
//