A Leaner, Cleaner Substrate

See allHide authors and affiliations

Science  23 Mar 2001:
Vol. 291, Issue 5512, pp. 2277
DOI: 10.1126/science.291.5512.2277a

Many antibiotics function by inhibiting the enzymes that synthesize the peptidoglycan layers that surround bacterial cell membranes. The bacterial transglycosylases are of special interest as targets because these enzymes are located on the outside surface of the cell, where they polymerize a cell wall constituent called Lipid II. One difficulty in studying transglycosylases is handling the substrate, which is hard to prepare in sufficient quantity and purity and which contains an undecaprenyl chain (55 carbon atoms) that aggregates. Ye et al. now report that they have identified a Lipid II analog with a shorter lipid chain (35 carbon atoms) that is a much better substrate for monitoring transglycosylase activity. This analog makes it possible to dispense with detergents in the in vitro reaction and should facilitate studies of these enzymes. — PDS

J. Am. Chem. Soc., in press.

Navigate This Article