OXLA_AGKCL
ID OXLA_AGKCL Reviewed; 19 AA.
AC P0CC16;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=L-amino-acid oxidase;
DE Short=ACL-LAO {ECO:0000303|PubMed:10441379};
DE Short=LAAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:10441379};
DE Flags: Fragment;
OS Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon
OS mokasen laticinctus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=37195;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR
RP LOCATION, AND SUBSTRATE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=10441379; DOI=10.1006/abbi.1999.1287;
RA Souza D.H.F., Eugenio L.M., Fletcher J.E., Jiang M.-S., Garratt R.C.,
RA Oliva G., Selistre-de-Araujo H.S.;
RT "Isolation and structural characterization of a cytotoxic L-amino acid
RT oxidase from Agkistrodon contortrix laticinctus snake venom: preliminary
RT crystallographic data.";
RL Arch. Biochem. Biophys. 368:285-290(1999).
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:10441379). Is active on L-Ile followed by L-Phe, L-Met,
CC L-Val, L-Arg, L-Leu (PubMed:10441379). Exhibits diverse biological
CC activities, such as hemorrhage (minimum hemorrhagic dose of 10 ug), and
CC apoptosis. May also induce hemolysis, edema, antibacterial and
CC antiparasitic activities. May also regulate platelet aggregation.
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:0000269|PubMed:10441379}.
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:10441379};
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:10441379};
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:10441379};
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:10441379};
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:10441379};
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:10441379};
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:10441379};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10441379};
CC Note=Does not use FAD as a cofactor. {ECO:0000269|PubMed:10441379};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000250|UniProtKB:P81382}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10441379}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10441379}.
CC -!- PTM: Contains 2 disulfide bonds. {ECO:0000250|UniProtKB:P81382}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0CC16; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
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:0044358; P:envenomation resulting in hemorrhagic damage in another organism; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Flavoprotein; FMN; Glycoprotein; Hemolysis;
KW Hemorrhagic toxin; Hemostasis impairing toxin; Oxidoreductase; Secreted;
KW Toxin.
FT CHAIN 1..>19
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000390926"
FT NON_TER 19
FT /evidence="ECO:0000303|PubMed:10441379"
SQ SEQUENCE 19 AA; 2375 MW; C1D709886B68E7B5 CRC64;
ADSRNPLEEE FRETNYEEF
