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P0C2D4 (OXLA_NAJKA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=K-LAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismNaja kaouthia (Monocled cobra) (Naja siamensis)
Taxonomic identifier8649 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

Protein attributes

Sequence length38 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (highly active against L-Phe and L-Tyr, and moderately active against L-Trp, L-Met, L-Leu, and L-Arg), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities By similarity. This protein inhibits both agonist- and shear stress-induced platelet aggregation (SIPA). Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Ref.2

Catalytic activity

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked. Ref.2

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.63 mM for L-Met Ref.2 Ref.3

KM=0.06 mM for L-Phe

KM=0.66 mM for L-Leu

KM=0.29 mM for L-Trp

pH dependence:

Optimum pH is 8.5, unlike many other venom L-amino acid oxidase, is also stable in alkaline medium.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›38›38L-amino-acid oxidase
PRO_0000273569

Amino acid modifications

Disulfide bond10 ↔ ? By similarity

Experimental info

Non-terminal residue381

Sequences

Sequence LengthMass (Da)Tools
P0C2D4 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: D988B9FC32DDDE08

FASTA384,514
        10         20         30 
DDRRSPLEEC FQQNDYEEFL EIAKNGLKKT XNPKHVXV 

« Hide

References

[1]"Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom."
Sakurai Y., Takatsuka H., Yoshioka A., Matsui T., Suzuki M., Titani K., Fujimura Y.
Toxicon 39:1827-1833(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Purification and properties of the L-amino acid oxidase from monocellate cobra (Naja naja kaouthia) venom."
Tan N.-H., Swaminathan S.
Int. J. Biochem. 24:967-973(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Tissue: Venom.
[3]"L-Amino acid oxidase from Naja naja oxiana venom."
Samel M., Tonismagi K., Ronnholm G., Vija H., Siigur J., Kalkkinen N., Siigur E.
Comp. Biochem. Physiol. 149:572-580(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP0C2D4.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_NAJKA
AccessionPrimary (citable) accession number: P0C2D4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families