Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents.

ABSTRACT: Methionine aminopeptidase (MetAP) is a class of ubiquitous enzymes essential for the survival of numerous bacterial species. These enzymes are responsible for the cleavage of N-terminal formyl-methionine initiators from nascent proteins to initiate post-translational modifications that are often essential to proper protein function. Thus, inhibition of MetAP activity has been implicated as a novel antibacterial target. We tested this idea in the present study by targeting the MetAP enzyme in the obligate intracellular pathogen Rickettsia prowazekii. We first identified potent RpMetAP inhibitory species by employing an in vitro enzymatic activity assay. The molecular docking program AutoDock was then utilized to compare published crystal structures of inhibited MetAP species to docked poses

SUBMITTER: Helgren TR 

PROVIDER: S-EPMC5319851 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature