OXLA_MACLB
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-AUG-2022, entry version 64.
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=0.40 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: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..>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
