OXLA_BOTJA
ID OXLA_BOTJA Reviewed; 37 AA.
AC P0DI88;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=L-amino-acid oxidase;
DE Short=BjarLAAO-I {ECO:0000303|PubMed:18346051};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:18346051, ECO:0000269|PubMed:19101583};
DE Flags: Fragment;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, CATALYTIC
RP ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=18346051; DOI=10.1111/j.1742-7843.2008.00229.x;
RA de Vieira Santos M.M., Sant'Ana C.D., Giglio J.R., da Silva R.J.,
RA Sampaio S.V., Soares A.M., Fecchio D.;
RT "Antitumoural effect of an L-amino acid oxidase isolated from Bothrops
RT jararaca snake venom.";
RL Basic Clin. Pharmacol. Toxicol. 102:533-542(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION, SUBCELLULAR LOCATION, AND
RP SUBSTRATE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=19101583; DOI=10.1016/j.toxicon.2008.12.004;
RA Ciscotto P., Machado de Avila R.A., Coelho E.A., Oliveira J., Diniz C.G.,
RA Farias L.M., de Carvalho M.A., Maria W.S., Sanchez E.F., Borges A.,
RA Chavez-Olortegui C.;
RT "Antigenic, microbicidal and antiparasitic properties of an L-amino acid
RT oxidase isolated from Bothrops jararaca snake venom.";
RL Toxicon 53:330-341(2009).
RN [3]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=20615423; DOI=10.1016/j.toxicon.2010.06.019;
RA Deolindo P., Teixeira-Ferreira A.S., DaMatta R.A., Alves E.W.;
RT "L-amino acid oxidase activity present in fractions of Bothrops jararaca
RT venom is responsible for the induction of programmed cell death in
RT Trypanosoma cruzi.";
RL Toxicon 56:944-955(2010).
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:18346051). Is highly active on L-Leu, L-Met, moderately
CC active on L-Arg, L-Trp, L-Phe, L-Val, L-His, and L-Ile, and is weakly
CC or not active on L-Cys, L-Lys, L-Ala, L-Thr, L-Asp, L-Ser, and L-Pro
CC (PubMed:18346051, PubMed:19101583). Exhibits diverse biological
CC activities, such as hemorrhage, edema, apoptosis of vascular
CC endothelial cells or tumor cell lines, as well as regulation of
CC platelet aggregation. Effects of snake L-amino oxidases on platelets
CC are controversial, since they either induce aggregation or inhibit
CC agonist-induced aggregation. These different effects are probably due
CC to different experimental conditions (By similarity). This protein
CC induce hemolysis and has antibacterial and antiparasitic activities
CC (against the Gram-positive S.aureus). Tested in vivo, this protein
CC significantly inhibits Ehrlich ascite tumors growth and induces an
CC influx of polymorphonuclear cells, as well as spontaneous liberation of
CC hydrogen peroxide from peritoneal macrophages.
CC {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:18346051,
CC ECO:0000269|PubMed:19101583, ECO:0000269|PubMed:20615423}.
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; Evidence={ECO:0000269|PubMed:18346051,
CC ECO:0000269|PubMed:19101583};
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:18346051,
CC ECO:0000269|PubMed:19101583};
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:18346051,
CC ECO:0000269|PubMed:19101583};
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:18346051,
CC ECO:0000269|PubMed:19101583};
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:18346051, ECO:0000269|PubMed:19101583};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2
CC + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146,
CC ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:18346051,
CC ECO:0000269|PubMed:19101583};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:18346051,
CC ECO:0000269|PubMed:19101583};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidine + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595,
CC ChEBI:CHEBI:58133; Evidence={ECO:0000269|PubMed:18346051,
CC ECO:0000269|PubMed:19101583};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-valine + O2 = 3-methyl-2-oxobutanoate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:61252, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57762; Evidence={ECO:0000269|PubMed:18346051,
CC ECO:0000269|PubMed:19101583};
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:18346051}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18346051,
CC ECO:0000269|PubMed:19101583}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18346051, ECO:0000305|PubMed:19101583}.
CC -!- PTM: N-Glycosylated. {ECO:0000269|PubMed:19101583}.
CC -!- MISCELLANEOUS: Has parasiticidal activities against both trypanosomes
CC and leishmania, as a result of enzyme-catalyzed hydrogen peroxide
CC production (PubMed:19101583, PubMed:20615423).
CC {ECO:0000269|PubMed:19101583, ECO:0000269|PubMed:20615423}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Bothrops jararaca venom seems to contain 2 isoforms with
CC different hydrophobic properties (PubMed:18346051). These isoforms may
CC reflect different glycosylation of the protein or they may have been
CC synthesized from different genes. {ECO:0000305|PubMed:18346051}.
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DR AlphaFoldDB; P0DI88; -.
DR SMR; P0DI88; -.
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; Secreted; Toxin.
FT CHAIN 1..>37
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000412595"
FT DISULFID 10..?
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_TER 37
FT /evidence="ECO:0000303|PubMed:18346051"
SQ SEQUENCE 37 AA; 4299 MW; 9C3BDE3E1E664AE7 CRC64;
ADDKNPLEEC FRETDYEEFL EIARNGLKAT SNPKRVV
