OXLA_NAJOX
ID OXLA_NAJOX Reviewed; 95 AA.
AC P0DI91;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=L-amino-acid oxidase;
DE Short=LAAO {ECO:0000303|PubMed:18294891};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:18294891};
DE Flags: Fragments;
OS Naja oxiana (Central Asian cobra) (Oxus cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8657;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=18294891; DOI=10.1016/j.cbpb.2007.11.008;
RA Samel M., Tonismagi K., Ronnholm G., Vija H., Siigur J., Kalkkinen N.,
RA Siigur E.;
RT "L-Amino acid oxidase from Naja naja oxiana venom.";
RL Comp. Biochem. Physiol. 149:572-580(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:18294891). Is highly active on L-Met, L-Leu, L-Phe, L-
CC Trp, and L-Arg, and no weakly or no active on L-His, L-Tyr, L-Ile, L-
CC Gln, and L-Lys (PubMed:18294891). Exhibits diverse biological
CC activities, such as antibacterial activity against both Gram-positive
CC (B.subtilis) and Gram-negative (E.coli) bacteria, and inhibition of
CC ADP- or collagen-induced platelet aggregation. Effects of snake L-amino
CC oxidases on platelets are controversial, since they either induce
CC aggregation or inhibit agonist-induced aggregation. These different
CC effects are probably due to different experimental conditions. This
CC protein may also induce hemorrhage, hemolysis, edema, apoptosis, and
CC have antiparasitic activities. {ECO:0000250|UniProtKB:P0CC17,
CC ECO:0000269|PubMed:18294891}.
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:18294891};
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:18294891};
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:18294891};
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:18294891};
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:18294891};
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:18294891};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.885 mM for L-Met {ECO:0000269|PubMed:18294891};
CC KM=0.75 mM for L-Leu {ECO:0000269|PubMed:18294891};
CC KM=0.147 mM for L-Trp {ECO:0000269|PubMed:18294891};
CC KM=0.051 mM for L-Phe {ECO:0000269|PubMed:18294891};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:18294891}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18294891}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18294891}.
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 AlphaFoldDB; P0DI91; -.
DR SABIO-RK; P0DI91; -.
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..>95
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000412604"
FT DISULFID 10..?
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID ?..89
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_CONS 25..26
FT /evidence="ECO:0000303|PubMed:18294891"
FT NON_CONS 34..35
FT /evidence="ECO:0000303|PubMed:18294891"
FT NON_CONS 56..57
FT /evidence="ECO:0000303|PubMed:18294891"
FT NON_CONS 69..70
FT /evidence="ECO:0000303|PubMed:18294891"
FT NON_TER 95
FT /evidence="ECO:0000303|PubMed:18294891"
SQ SEQUENCE 95 AA; 11216 MW; EFD6FF44B5FFF34A CRC64;
DDRRSPLEEC FQQNDYEEFL EIARNSQLYQ ESLREDSSYH LSFIESLKSD ALFSYEKKFW
EADGIHGGKV INDLSLIHDL PKREIQALCY PSIKK
