OXLA_BOTAL
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 25-MAY-2022, entry version 23.
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:0044179; P:hemolysis in 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
