Structural highlights
Function
OXLA_NAJAT Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:18180850). Shows activity on L-Leu (PubMed:18180850). 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 induces platelet aggregation by both hydrogen peroxide production and binding to platelet membrane proteins (that would enhance the sensitivity of platelets to hydrogen peroxide). 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.[UniProtKB:P0CC17][1]
See Also
References
- ↑ Li R, Zhu S, Wu J, Wang W, Lu Q, Clemetson KJ. L-amino acid oxidase from Naja atra venom activates and binds to human platelets. Acta Biochim Biophys Sin (Shanghai). 2008 Jan;40(1):19-26. PMID:18180850 doi:10.1111/j.1745-7270.2008.00372.x
