Crystal structure of Schistosoma mansoni arginase, a potential drug target for the treatment of schistosomiasis.

ABSTRACT: The X-ray crystal structure of arginase from Schistosoma mansoni (SmARG) and the structures of its complexes with several amino acid inhibitors have been determined at atomic resolution. SmARG is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to form l-ornithine and urea, and this enzyme is upregulated in all forms of the parasite that interact with the human host. Current hypotheses suggest that parasitic arginases could play a role in host immune evasion by depleting pools of substrate l-arginine that would otherwise be utilized for NO biosynthesis and NO-dependent processes in the immune response. Although the amino acid sequence of SmARG is only 42% identical with that of human arginase I, residues important for substrate binding and catalysis are stric

SUBMITTER: Hai Y 

PROVIDER: S-EPMC4138072 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature