Biochemical characterization of aminopeptidase N2 from Toxoplasma gondii.

ABSTRACT: Aminopeptidase N (APN) is a member of the highly conserved M1 family of metalloproteases, and is considered to be a valuable target for the treatment of a variety of diseases, e.g., cancer, malaria, and coccidiosis. In this study, we identified an APN gene (TgAPN2) in the Toxoplasma gondii genome, and performed a biochemical characterization of the recombinant TgAPN2 (rTgAPN2) protein. Active rTgAPN2 was first produced and purified in Escherichia coli. The catalytic activity of the enzyme was verified using a specific fluorescent substrate, H-Ala-MCA; the rTgAPN2 was relatively active in the absence of added metal ions. The addition of some metal ions, especially Zn²⁺, inhibited the activity of the recombinant enzyme. The activity of rTgAPN2 was reduced in the presence of the ED

SUBMITTER: Li Q 

PROVIDER: S-EPMC5573830 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature