Ontology highlight
ABSTRACT:
SUBMITTER: Carney DW
PROVIDER: S-EPMC4992462 | biostudies-literature | 2015 Sep
REPOSITORIES: biostudies-literature
Carney Daniel W DW Schmitz Karl R KR Scruse Anthony C AC Sauer Robert T RT Sello Jason K JK
Chembiochem : a European journal of chemical biology 20150727 13
The cyclic acyldepsipeptide (ADEP) antibiotics act by binding the ClpP peptidase and dysregulating its activity. Their exocyclic N-acylphenylalanine is thought to structurally mimic the ClpP-binding, (I/L)GF tripeptide loop of the peptidase's accessory ATPases. We found that ADEP analogues with exocyclic N-acyl tripeptides or dipeptides resembling the (I/L)GF motif were weak ClpP activators and had no bioactivity. In contrast, ADEP analogues possessing difluorophenylalanine N-capped with methyl- ...[more]