OXLA_VIPBB
ID OXLA_VIPBB Reviewed; 88 AA.
AC P0C2D7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=L-amino-acid oxidase;
DE Short=LAAO {ECO:0000303|PubMed:16574513};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:16574513};
DE Flags: Fragments;
OS Vipera berus berus (Common viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=31156;
RN [1]
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=16574513; DOI=10.1016/j.bbapap.2006.01.021;
RA Samel M., Vija H., Ronnholm G., Siigur J., Kalkkinen N., Siigur E.;
RT "Isolation and characterization of an apoptotic and platelet aggregation
RT inhibiting L-amino acid oxidase from Vipera berus berus (common viper)
RT venom.";
RL Biochim. Biophys. Acta 1764:707-714(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:16574513). Is highly active on L-Met, L-Leu, L-Phe, L-
CC Ile, and L-Arg, moderately active on L-His, L-Trp, L-Asn, L-Glu, and L-
CC Val, and weakly or not active on L-Gln, L-Lys, L-Asp, L-Ala, L-Tyr, L-
CC Ser, L-Pro, L-Gly, L-Thr, and L-Cys (PubMed:16574513). Exhibits diverse
CC biological activities, such as hemorrhage, hemolysis, edema, apoptosis
CC of vascular endothelial cells or tumor cell lines, antibacterial and
CC antiparasitic activities (By similarity). In addition, this protein has
CC an ability to induce apoptosis in cultured HeLa and K562 cells, and
CC inhibits ADP-induced platelet aggregation dose-dependently. Effects of
CC snake L-amino oxidases on platelets are controversial, since they
CC either induce aggregation or inhibit agonist-induced aggregation. These
CC different effects are probably due to different experimental
CC conditions. {ECO:0000250|UniProtKB:P0CC17,
CC ECO:0000269|PubMed:16574513}.
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:16574513};
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:16574513};
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:16574513};
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:16574513};
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:16574513};
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:16574513};
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:16574513};
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:16574513};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine + O2 = 2-oxosuccinamate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:61224, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57735,
CC ChEBI:CHEBI:58048; Evidence={ECO:0000269|PubMed:16574513};
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:16574513};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + O2 = 2-oxoglutarate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:20728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:16574513};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.361 mM for L-Leu {ECO:0000269|PubMed:16574513};
CC KM=0.286 mM for L-Met {ECO:0000269|PubMed:16574513};
CC KM=0.058 mM for L-Phe {ECO:0000269|PubMed:16574513};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:16574513}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16574513}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:16574513}.
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; P0C2D7; -.
DR SMR; P0C2D7; -.
DR SABIO-RK; P0C2D7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050025; F:L-glutamate oxidase activity; IEA:RHEA.
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..>88
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000273573"
FT BINDING 74
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 81..86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 81..82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 10..?
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_CONS 37..38
FT /evidence="ECO:0000303|PubMed:16574513"
FT NON_CONS 44..45
FT /evidence="ECO:0000303|PubMed:16574513"
FT NON_CONS 52..53
FT /evidence="ECO:0000303|PubMed:16574513"
FT NON_CONS 61..62
FT /evidence="ECO:0000303|PubMed:16574513"
FT NON_CONS 68..69
FT /evidence="ECO:0000303|PubMed:16574513"
FT NON_TER 88
FT /evidence="ECO:0000303|PubMed:16574513"
SQ SEQUENCE 88 AA; 10295 MW; D2A63168391A7965 CRC64;
ADDKNPLEEC FREDDYEEFL EIAKNGLKKT SNPKHIVYPV KPSEQLYEES LRDQLPTSMH
RYPSMIQKIF FAGEYTANAH GWIDSTIK
