OXLA1_DABRR
ID OXLA1_DABRR Reviewed; 20 AA.
AC P86535;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=L-amino-acid oxidase L1 {ECO:0000303|PubMed:18384385};
DE Short=LAAO-L1 {ECO:0000303|PubMed:18384385};
DE Short=LAO {ECO:0000303|PubMed:20203422};
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, CATALYTIC ACTIVITY, GLYCOSYLATION, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INHIBITION BY SUBSTRATE ANALOGS,
RP SUBCELLULAR 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).
RN [2]
RP PROTEIN SEQUENCE OF 1-19, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=20203422; DOI=10.2220/biomedres.31.71;
RA Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G.,
RA Athauda S.B., Moriyama A.;
RT "Molecular diversity in venom proteins of the Russell's viper (Daboia
RT russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka.";
RL Biomed. Res. 31:71-81(2010).
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-Met, L-Ile, L-Leu, 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=0.297 mM for L-Met {ECO:0000269|PubMed:18384385};
CC KM=1.44 mM for L-Ile {ECO:0000269|PubMed:18384385};
CC KM=0.750 mM for L-Leu {ECO:0000269|PubMed:18384385};
CC KM=0.066 mM for L-Phe {ECO:0000269|PubMed:18384385};
CC KM=0.210 mM for L-Trp {ECO:0000269|PubMed:18384385};
CC KM=0.052 mM for L-Tyr {ECO:0000269|PubMed:18384385};
CC Vmax=8.96 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 ECO:0000269|PubMed:20203422}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18384385, ECO:0000305|PubMed:20203422}.
CC -!- PTM: N-glycosylated. {ECO:0000305|PubMed:18384385}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000255}.
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DR AlphaFoldDB; P86535; -.
DR SABIO-RK; P86535; -.
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 L1"
FT /id="PRO_0000394725"
FT DISULFID 10..?
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT CONFLICT 4
FT /note="I -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="K -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="F -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="Y -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 20
FT /evidence="ECO:0000303|PubMed:18384385"
SQ SEQUENCE 20 AA; 2519 MW; 999C77D7C86348E7 CRC64;
ADDINPKEEC FFEDDYYEFE
