Structural highlights
Function
[OXLA_GLOBL] 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. Exhibits diverse biological activities, such as apoptosis, and inhibition of 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. This protein may also induce hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Takatsuka H, Sakurai Y, Yoshioka A, Kokubo T, Usami Y, Suzuki M, Matsui T, Titani K, Yagi H, Matsumoto M, Fujimura Y. Molecular characterization of L-amino acid oxidase from Agkistrodon halys blomhoffii with special reference to platelet aggregation. Biochim Biophys Acta. 2001 Jan 12;1544(1-2):267-77. PMID:11341935
- ↑ Suhr SM, Kim DS. Identification of the snake venom substance that induces apoptosis. Biochem Biophys Res Commun. 1996 Jul 5;224(1):134-9. PMID:8694800 doi:http://dx.doi.org/S0006-291X(96)90996-1
