OXLA_NAJKA
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 25-MAY-2022, entry version 41.
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=5.0 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}.
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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: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..>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
