| Literature DB >> 6222035 |
D Mengin-Lecreulx, B Flouret, J van Heijenoort.
Abstract
A high-pressure liquid chromatography procedure was developed for the isolation and quantitation of UDP-N-acetylglucosamine, UDP-N-acetylglucosamine-enolpyruvate, and UDP-N-acetylmuramic acid, which are the early cytoplasmic precursors of bacterial peptidoglycan. In exponential-phase cells of Escherichia coli K-12, the intracellular concentration of UDP-N-acetylglucosamine was about 100 microM, whereas that of UDP-N-acetylglucosamine-enolpyruvate was only 2 microM. The phosphoenolpyruvate: UDP-N-acetylglucosamine transferase and UDP-N-acetylglucosamine-enolpyruvate reductase activities were investigated in extracts from E. coli. These activities appeared to be present in amounts sufficient for the ongoing rate of peptidoglycan synthesis. Certain uridine nucleotide peptidoglycan precursors were found to inhibit phosphoenolpyruvate: UDP-N-acetylglucosamine transferase activity.Entities:
Mesh:
Substances:
Year: 1983 PMID: 6222035 PMCID: PMC217602 DOI: 10.1128/jb.154.3.1284-1290.1983
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490