Ontology highlight
ABSTRACT:
SUBMITTER: Helgren TR
PROVIDER: S-EPMC5908248 | biostudies-literature | 2018 May
REPOSITORIES: biostudies-literature
Bioorganic & medicinal chemistry letters 20180315 8
Methionine aminopeptidase (MetAP) is a dinuclear metalloprotease responsible for the cleavage of methionine initiator residues from nascent proteins. MetAP activity is necessary for bacterial proliferation and is therefore a projected novel antibacterial target. A compound library consisting of 294 members containing metal-binding functional groups was screened against Rickettsia prowazekii MetAP to determine potential inhibitory motifs. The compounds were first screened against the target at a ...[more]