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   03-AUG-2022, entry version 57.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=Casca LAO {ECO:0000303|PubMed:16307769};
DE            Short=LAAO;
DE            EC=1.4.3.2 {ECO:0000269|PubMed:16307769};
DE   Flags: Fragment;
OS   Crotalus durissus cascavella (Northeastern Brazilian rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=184540;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
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 cascavella
RT   venom.";
RL   Toxicon 47:47-57(2006).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids, thus producing hydrogen
CC       peroxide that may contribute to the diverse toxic effects of this
CC       enzyme (PubMed:16307769). Shows activity on L-Leu (PubMed:16307769).
CC       Exhibits diverse biological activities, such as apoptosis,
CC       antibacterial activities against both Gram-negative and Gram-positive
CC       bacteria and antiparasitic activities, as well as induction of platelet
CC       aggregation (PubMed:16307769). Effects of snake L-amino oxidases on
CC       platelets are controversial, since they either induce aggregation or
CC       inhibit agonist-induced aggregation (By similarity). These different
CC       effects are probably due to different experimental conditions (By
CC       similarity). This protein may also induce hemorrhage, hemolysis, and
CC       edema (By similarity). {ECO:0000250|UniProtKB:P0CC17,
CC       ECO:0000269|PubMed:16307769}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:59869; EC=1.4.3.2;
CC         Evidence={ECO:0000269|PubMed:16307769};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:16307769};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:16307769};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=46.7 uM for L-Leu {ECO:0000269|PubMed:16307769};
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:16307769};
CC   -!- SUBUNIT: Homodimer; non-covalently linked.
CC       {ECO:0000269|PubMed:16307769}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16307769}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:16307769}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC   -!- MISCELLANEOUS: Has parasiticidal activities against leishmania, as a
CC       result of enzyme-catalyzed hydrogen peroxide production.
CC       {ECO:0000305|PubMed:16307769}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C2D2; -.
DR   SMR; P0C2D2; -.
DR   PRIDE; P0C2D2; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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 another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW   Hemostasis impairing toxin; Oxidoreductase;
KW   Platelet aggregation activating toxin; Secreted; Toxin.
FT   CHAIN           1..>61
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000273567"
FT   BINDING         43..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   DISULFID        10..?
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   NON_TER         61
FT                   /evidence="ECO:0000303|PubMed:16307769"
SQ   SEQUENCE   61 AA;  6561 MW;  9D7F04E64267A122 CRC64;
     ADDRNPLEQC FRETDYEEFL EIARNNLKAT SNPKHVVIVG AGMAGLSAAY VLSGGGHQVT
     V