ID   OXLA_MACLB              Reviewed;         107 AA.
AC   P81375;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-MAY-2023, entry version 66.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO {ECO:0000303|PubMed:16828829};
DE            Short=LAO;
DE            EC=1.4.3.2 {ECO:0000269|PubMed:16828829};
DE   Flags: Fragments;
OS   Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX   NCBI_TaxID=8709;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-27.
RC   TISSUE=Venom;
RA   Tan C.H., Ang W.C.;
RL   Submitted (MAY-1998) to UniProtKB.
RN   [2]
RP   PROTEIN SEQUENCE OF 27-107, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL
RP   PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY,
RP   SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=16828829; DOI=10.1016/j.toxicon.2006.05.004;
RA   Tonismagi K., Samel M., Trummal K., Ronnholm G., Siigur J., Kalkkinen N.,
RA   Siigur E.;
RT   "L-amino acid oxidase from Vipera lebetina venom: isolation,
RT   characterization, effects on platelets and bacteria.";
RL   Toxicon 48:227-237(2006).
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:16828829). Shows high activity on L-Met, moderate
CC       activity on L-Trp, L-Leu, L-His, L-Phe, L-Arg, L-Ile, low activity on
CC       L-Val, L-Glu, L-Lys, L-Gln, L-Asn, L-Tyr, L-Ala, and no activity on L-
CC       Asp, L-Ser, L-Pro, L-Gly, L-Thr and L-Cys (PubMed:16828829). Shows
CC       antimicrobial activity inhibiting the growth of both Gram-negative and
CC       Gram-positive bacteria (PubMed:16828829). Also inhibits platelet
CC       aggregation induced by ADP or collagen (PubMed:16828829). Effects of
CC       snake L-amino oxidases on platelets are controversial, since they
CC       either induce aggregation or inhibit agonist-induced aggregation (By
CC       similarity). These different effects are probably due to different
CC       experimental conditions (By similarity). This protein may also induce
CC       hemorrhage, hemolysis, edema, apoptosis, and have antiparasitic
CC       activities (By similarity). {ECO:0000250|UniProtKB:P0CC17,
CC       ECO:0000269|PubMed:16828829}.
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:16828829};
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:16828829};
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:16828829};
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:16828829};
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:16828829};
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:16828829};
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:16828829};
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:16828829};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P81382};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.4 mM for L-Leu {ECO:0000269|PubMed:16828829};
CC         KM=0.65 mM for L-Met {ECO:0000269|PubMed:16828829};
CC         KM=0.17 mM for L-Trp {ECO:0000269|PubMed:16828829};
CC       Temperature dependence:
CC         Thermostable between 4 and 25 degrees Celsius. At -20 degrees
CC         Celsius, the remaining activity is 20%. Heating at 70 degrees Celsius
CC         inactivates the enzyme in 15 minutes. {ECO:0000269|PubMed:16828829};
CC   -!- SUBUNIT: Homodimer; non-covalently linked.
CC       {ECO:0000269|PubMed:16828829}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16828829}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:16828829}.
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; P81375; -.
DR   SMR; P81375; -.
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.
DR   Gene3D; 3.90.660.10; -; 1.
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..>107
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000099872"
FT   BINDING         35..38
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   DISULFID        10..?
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000303|PubMed:16828829"
FT   NON_CONS        38..39
FT                   /evidence="ECO:0000303|PubMed:16828829"
FT   NON_CONS        48..49
FT                   /evidence="ECO:0000303|PubMed:16828829"
FT   NON_CONS        57..58
FT                   /evidence="ECO:0000303|PubMed:16828829"
FT   NON_CONS        67..68
FT                   /evidence="ECO:0000303|PubMed:16828829"
FT   NON_CONS        79..80
FT                   /evidence="ECO:0000303|PubMed:16828829"
FT   NON_CONS        90..91
FT                   /evidence="ECO:0000303|PubMed:16828829"
FT   NON_TER         107
FT                   /evidence="ECO:0000303|PubMed:16828829"
SQ   SEQUENCE   107 AA;  12435 MW;  576D2F829779B412 CRC64;
     ADDKNPLEEC FREDDYEEFL EIAKNGLEGW YANLGPMRYP VKPSEEGKHD DIFAYEKFDE
     IVGGMDKKFW EDDGIHGGKE TFCYSPMIQK PYQFQHFSEA LTAPVGR
//