Chemoenzymatic syntheses of water-soluble lipid I fluorescent probes.

ABSTRACT: Peptidoglycan (PG) is unique to bacteria, and thus, the enzymes responsible for its biosynthesis are promising antibacterial drug targets. The membrane-embedded enzymes in PG remain significant challenges in studying their mechanisms due to the fact that preparations of suitable enzymatic substrates require time-consuming biological transformations or chemical synthesis. Lipid I (prenyl diphosphoryl-MurNAc-pentapeptide) is an important PG biosynthesis intermediate to study the central enzymes, translocase I (MraY/MurX) and MurG. Lipid I isolated from nature contains the C₅₀-or C₅₅-prenyl unit that shows extremely poor water-solubility that renders studies of translocase I and MurG enzymes difficult. We have studied biological transformation of water soluble lipid I fl

SUBMITTER: Mitachi K 

PROVIDER: S-EPMC4505380 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature