ID   OXLA_BOTAL              Reviewed;          18 AA.
AC   P0DI86;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-MAY-2023, entry version 24.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=Balt-LAAO-I {ECO:0000303|PubMed:15142548};
DE            Short=LAO;
DE            EC=1.4.3.2 {ECO:0000269|PubMed:15142548};
DE   Flags: Fragment;
OS   Bothrops alternatus (Urutu) (Rhinocerophis alternatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=64174;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP   AND SUBSTRATE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=15142548; DOI=10.1016/j.bmc.2004.03.049;
RA   Stabeli R.G., Marcussi S., Carlos G.B., Pietro R.C.,
RA   Selistre-de-Araujo H.S., Giglio J.R., Oliveira E.B., Soares A.M.;
RT   "Platelet aggregation and antibacterial effects of an L-amino acid oxidase
RT   purified from Bothrops alternatus snake venom.";
RL   Bioorg. Med. Chem. 12:2881-2886(2004).
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:15142548). Is highly active on L-Phe > L-Tyr > L-Met >
CC       L-Leu, and is weakly or not active on other amino acids
CC       (PubMed:15142548). Exhibits diverse biological activities, such as
CC       slight hemorrhage, induction of platelet aggregation, edema in the
CC       mouse paw and bactericidal activity against both Gram-positive
CC       (S.aureus) and Gram-negative (E.coli) bacteria (PubMed:15142548). May
CC       also induce hemolysis, apoptosis of vascular endothelial cells or tumor
CC       cell lines, and may have antiparasitic activities (By similarity).
CC       Effects of snake L-amino oxidases on platelets are controversial, since
CC       they either induce aggregation or inhibit agonist-induced aggregation.
CC       These different effects are probably due to different experimental
CC       conditions. {ECO:0000250, ECO:0000269|PubMed:15142548}.
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:15142548};
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:15142548};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:15142548};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate +
CC         H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57844;
CC         Evidence={ECO:0000269|PubMed:15142548};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242,
CC         ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:15142548};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P81382};
CC   -!- SUBUNIT: Homodimer; non-covalently linked.
CC       {ECO:0000269|PubMed:15142548}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15142548}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15142548}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000250|UniProtKB:P81382}.
CC   -!- PTM: N-glycosylated. The enzymatic activity is not affected by
CC       deglycosylation. {ECO:0000269|PubMed:15142548}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: The existence of several isoforms has been reported that may
CC       be due to either different composition or different glycosylation or by
CC       the synthesis from different genes. {ECO:0000305|PubMed:15142548}.
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DR   AlphaFoldDB; P0DI86; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW   Hemorrhagic toxin; Hemostasis impairing toxin; Oxidoreductase;
KW   Platelet aggregation activating toxin; Secreted; Toxin.
FT   CHAIN           1..>18
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000412593"
FT   NON_TER         18
FT                   /evidence="ECO:0000303|PubMed:15142548"
SQ   SEQUENCE   18 AA;  2195 MW;  CA5F483463FD1ADC CRC64;
     ADVRNPLEEF RETDYEVL
//