Abstract
Abstract The particulate enzyme preparation from cells of Micrococcus lysodeikticus which catalyzes peptidoglycan synthesis contains both enzyme proteins and an essential phospholipid which acts as a carrier of sugar fragments during peptidoglycan synthesis. This enzyme preparation has been separated into its protein and lipid components by extraction with chloroform-methanol (1:1) at -17°. The enzyme protein and phospholipid have been reconstituted in the presence of deoxycholate at low concentrations. The endogenous phospholipid acceptors have been labeled with 32P and then separated from other 32P-phospholipids by thin layer chromatography in several solvents. Two 32-P-phospholipid fractions were separated, each of which could be converted to the 32P-phospholipid intermediate, disaccharide(-pentapeptide)-P-P-phospholipid, in the presence of uridine diphosphate acetylmuramyl-pentapeptide and UDP-acetylglucosamine.
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