Structural and Biochemical Characterization of Apicomplexan Inorganic Pyrophosphatases.

ABSTRACT: Inorganic pyrophosphatases (PPase) participate in energy cycling and they are essential for growth and survival of organisms. Here we report extensive structural and functional characterization of soluble PPases from the human parasites Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase). Our results show that PfPPase is a cytosolic enzyme whose gene expression is upregulated during parasite asexual stages. Cambialistic PfPPase actively hydrolyzes linear short chain polyphosphates like PP_i, polyP₃ and ATP in the presence of Zn²⁺. A remarkable new feature of PfPPase is the low complexity asparagine-rich N-terminal region that mediates its dimerization. Deletion of N-region has an unexpected and substantial effect on the stability of PfPPase domai

SUBMITTER: Jamwal A 

PROVIDER: S-EPMC5507929 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature