ID OXLA_NAJKA Reviewed; 38 AA. AC P0C2D4; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 03-MAY-2023, entry version 43. DE RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:11600144, ECO:0000303|PubMed:1612186}; DE Short=K-LAO {ECO:0000303|PubMed:11600144}; DE Short=LAAO {ECO:0000303|PubMed:1612186}; DE EC=1.4.3.2 {ECO:0000269|PubMed:1612186}; DE Flags: Fragment; OS Naja kaouthia (Monocled cobra) (Naja siamensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja. OX NCBI_TaxID=8649; RN [1] RP PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION. RC TISSUE=Venom; RX PubMed=11600144; DOI=10.1016/s0041-0101(01)00133-7; RA Sakurai Y., Takatsuka H., Yoshioka A., Matsui T., Suzuki M., Titani K., RA Fujimura Y.; RT "Inhibition of human platelet aggregation by L-amino acid oxidase purified RT from Naja naja kaouthia venom."; RL Toxicon 39:1827-1833(2001). RN [2] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBSTRATE SPECIFICITY, RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RC TISSUE=Venom; RX PubMed=1612186; DOI=10.1016/0020-711x(92)90105-a; RA Tan N.-H., Swaminathan S.; RT "Purification and properties of the L-amino acid oxidase from monocellate RT cobra (Naja naja kaouthia) venom."; RL Int. J. Biochem. 24:967-973(1992). 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:1612186). Is very active against L-Phe and L-Tyr, CC moderately active against L-Trp, L-Met, L-Leu, L-norleucine (L-2- CC aminohexanoate), L-Arg and L-norvaline (L-2-aminopentanoate), and CC slightly active against L-His, L-cystine, and L-Ile (PubMed:1612186). CC L-Gln, L-Lys, L-Asn, L-ornithine, L-Ala and L-Val are oxidized very CC slowly (PubMed:1612186). Exhibits diverse biological activities, such CC as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial CC cells or tumor cell lines, antibacterial and antiparasitic activities CC (By similarity). This protein inhibits both agonist- and shear stress- CC induced platelet aggregation (SIPA) (PubMed:11600144). Effects of snake CC L-amino oxidases on platelets are controversial, since they either CC induce aggregation or inhibit agonist-induced aggregation. These CC different effects are probably due to different experimental CC conditions. {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:11600144, CC ECO:0000269|PubMed:1612186}. 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; Evidence={ECO:0000269|PubMed:1612186}; 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:1612186}; 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:1612186}; 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:1612186}; 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:1612186}; 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:1612186}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-2-aminohexanoate + O2 = 2-oxohexanoate + H2O2 + CC NH4(+); Xref=Rhea:RHEA:61268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35177, CC ChEBI:CHEBI:58455; Evidence={ECO:0000269|PubMed:1612186}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-2-aminopentanoate + O2 = 2-oxopentanoate + H2O2 + CC NH4(+); Xref=Rhea:RHEA:61272, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28644, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:58441; Evidence={ECO:0000269|PubMed:1612186}; 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:1612186}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P81382}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.023 mM for L-Tyr {ECO:0000269|PubMed:1612186}; CC KM=0.06 mM for L-Phe {ECO:0000269|PubMed:1612186}; CC KM=0.29 mM for L-Trp {ECO:0000269|PubMed:1612186}; CC KM=0.63 mM for L-Met {ECO:0000269|PubMed:1612186}; CC KM=0.66 mM for L-Leu {ECO:0000269|PubMed:1612186}; CC KM=1.69 mM for L-Arg {ECO:0000269|PubMed:1612186}; CC KM=2.86 mM for L-Cys {ECO:0000269|PubMed:1612186}; CC KM=5 mM for L-Ile {ECO:0000269|PubMed:1612186}; CC KM=5.49 mM for L-His {ECO:0000269|PubMed:1612186}; CC KM=11.59 mM for L-Asp {ECO:0000269|PubMed:1612186}; CC pH dependence: CC Optimum pH is 8.5, unlike many other venom L-amino acid oxidase, is CC also stable in alkaline medium. {ECO:0000269|PubMed:1612186}; CC -!- SUBUNIT: Homodimer; non-covalently linked. CC {ECO:0000269|PubMed:1612186}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11600144, CC ECO:0000269|PubMed:1612186}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:11600144, ECO:0000305|PubMed:1612186}. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}. 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 SABIO-RK; P0C2D4; -. 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. DR Gene3D; 3.90.660.10; -; 1. 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..>38 FT /note="L-amino-acid oxidase" FT /id="PRO_0000273569" FT DISULFID 10..? FT /evidence="ECO:0000250|UniProtKB:P81382" FT NON_TER 38 FT /evidence="ECO:0000303|PubMed:11600144" SQ SEQUENCE 38 AA; 4514 MW; D988B9FC32DDDE08 CRC64; DDRRSPLEEC FQQNDYEEFL EIAKNGLKKT XNPKHVXV //