OXLA2_DABRR
ID OXLA2_DABRR Reviewed; 20 AA.
AC P0DI90;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=L-amino-acid oxidase L2 {ECO:0000303|PubMed:18384385};
DE Short=LAAO-L2 {ECO:0000303|PubMed:18384385};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:18384385};
DE Flags: Fragment;
OS Daboia russelii (Russel's viper) (Vipera russelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=8707;
RN [1]
RP PROTEIN SEQUENCE, GLYCOSYLATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, INHIBITION BY SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND SUBSTRATE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=18384385; DOI=10.1111/j.1742-4658.2008.06362.x;
RA Mandal S., Bhattacharyya D.;
RT "Two L-amino acid oxidase isoenzymes from Russell's viper (Daboia russelli
RT russelli) venom with different mechanisms of inhibition by substrate
RT analogs.";
RL FEBS J. 275:2078-2095(2008).
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:18384385). Is active on L-Ile, L-Leu, L-Met, L-Phe, L-
CC Trp, and L-Tyr (PubMed:18384385). Exhibits diverse biological
CC activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular
CC endothelial cells or tumor cell lines, antibacterial and antiparasitic
CC activities, as well as regulation of platelet aggregation. Its effect
CC on platelets is controversial, since it either induces aggregation or
CC inhibits agonist-induced aggregation. These different effects are
CC probably due to different experimental conditions. {ECO:0000250,
CC ECO:0000269|PubMed:18384385}.
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:18384385};
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:18384385};
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:18384385};
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:18384385};
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:18384385};
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:18384385};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:18384385};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:18384385};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.89 mM for L-Ile {ECO:0000269|PubMed:18384385};
CC KM=599.7 uM for L-Leu {ECO:0000269|PubMed:18384385};
CC KM=222.8 uM for L-Met {ECO:0000269|PubMed:18384385};
CC KM=49.3 uM for L-Phe {ECO:0000269|PubMed:18384385};
CC KM=235.1 uM for L-Trp {ECO:0000269|PubMed:18384385};
CC KM=538.2 uM for L-Tyr {ECO:0000269|PubMed:18384385};
CC Vmax=6.94 umol/min/mg enzyme toward L-Phe
CC {ECO:0000269|PubMed:18384385};
CC -!- SUBUNIT: Monomer (Probable). This is in contrast with most of its
CC orthologs, that are non-covalently linked homodimers.
CC {ECO:0000269|PubMed:18384385, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18384385}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18384385}.
CC -!- PTM: N-glycosylated. {ECO:0000305|PubMed:18384385}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DI90; -.
DR SABIO-RK; P0DI90; -.
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..>20
FT /note="L-amino-acid oxidase L2"
FT /id="PRO_0000412601"
FT DISULFID 10..?
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_TER 20
FT /evidence="ECO:0000303|PubMed:18384385"
SQ SEQUENCE 20 AA; 2310 MW; 9D194277D99593E7 CRC64;
ADDKNPLEEC FCEDDDYCEG
