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 03-MAY-2023, entry version 23. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:0031640; P:killing of cells of 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 //