OXLA_BOTLC
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 25-MAY-2022, entry version 22.
DE RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:21539897};
DE Short=Bl-LAAO {ECO:0000303|PubMed:21539897};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000303|PubMed:21539897};
DE Flags: Fragment;
OS Bothrops leucurus (Whitetail lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157295;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP GLYCOSYLATION, MASS SPECTROMETRY, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
RP AND SUBSTRATE SPECIFICITY.
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., de Rezende F.F.,
RA Eble J.A., Sanchez E.F.;
RT "Cytotoxicity and inhibition of platelet aggregation caused by an l-amino
RT 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, thus producing hydrogen
CC peroxide that may contribute to the diverse toxic effects of this
CC enzyme (PubMed:21539897). Is highly active against L-Met, L-Leu, L-
CC norleucine (L-2-aminohexanoate), L-Trp, L-Phe, moderately active
CC against L-Tyr, and no active on L-Gly, L-Ala, L-Val, L-Pro, L-His, L-
CC Lys, L-Arg, L-Asp, L-Asn, L-Gln, L-Glu, L-Ser, and L-Thr
CC (PubMed:21539897). Exhibits diverse biological activities, such as
CC hemorrhage, hemolysis, edema, antibacterial and antiparasitic
CC activities (By similarity). In addition, this protein induces
CC apoptosis. It also interacts with endothelial cells, and inhibits
CC collagen- and ADP-induced platelet aggregation. L-LAAO family effects
CC on platelets are controversial, since it either induces aggregation or
CC inhibits agonist-induced aggregation. These different effects are
CC probably due to different experimental conditions.
CC {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:21539897}.
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:21539897};
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:21539897};
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:21539897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+);
CC Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:21539897};
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:21539897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-2-aminohexanoate + O2 = 2-oxohexanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35177,
CC ChEBI:CHEBI:58455; Evidence={ECO:0000269|PubMed:21539897};
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:21539897};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-8.8 for L-Leu. {ECO:0000269|PubMed:21539897};
CC -!- SUBUNIT: Monomer. This is in contrast with most of its orthologs, that
CC are non-covalently linked homodimers. {ECO:0000269|PubMed:21539897}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21539897}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:21539897}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:21539897}.
CC -!- MASS SPECTROMETRY: Mass=57000; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21539897};
CC -!- MISCELLANEOUS: Has parasiticidal activities against both trypanosomes
CC and leishmania, as a result of enzyme-catalyzed hydrogen peroxide
CC production. {ECO:0000305|PubMed:21539897}.
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:21539897}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DI89; -.
DR SMR; P0DI89; -.
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 Hemostasis impairing toxin; Oxidoreductase;
KW Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN 1..>30
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000412596"
FT DISULFID 10..?
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_TER 30
FT /evidence="ECO:0000303|PubMed:21539897"
SQ SEQUENCE 30 AA; 3507 MW; 37BCDB4946D486E0 CRC64;
ADDRNPLEEC FRETDYEEFL EIAKNGLSTT
