Structural highlights
Function
ARGI_ENTH1 Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis (PubMed:15053781, PubMed:29691540, PubMed:31199070). By depleting host L-arginine, a substrate for nitric oxide synthase (NOS), prevents the production of nitric oxide (NO) by host activated macrophages, and thus allows the parasite to evade host immune response (PubMed:15053781).[1] [2] [3]
See Also
References
- ↑ Elnekave K, Siman-Tov R, Ankri S. Consumption of L-arginine mediated by Entamoeba histolytica L-arginase (EhArg) inhibits amoebicidal activity and nitric oxide production by activated macrophages. Parasite Immunol. 2003 Nov-Dec;25(11-12):597-608. PMID:15053781 doi:10.1111/j.0141-9838.2004.00669.x
- ↑ Malik A, Singh H, Pareek A, Tomar S. Biochemical and biophysical insights into the metal binding spectrum and bioactivity of arginase of Entamoeba histolytica. Metallomics. 2018 Apr 25;10(4):623-638. PMID:29691540 doi:10.1039/c8mt00002f
- ↑ Malik A, Dalal V, Ankri S, Tomar S. Structural insights into Entamoeba histolytica arginase and structure-based identification of novel non-amino acid based inhibitors as potential antiamoebic molecules. FEBS J. 2019 Jun 14. doi: 10.1111/febs.14960. PMID:31199070 doi:http://dx.doi.org/10.1111/febs.14960