Synthesis of peptidoglycan in the form of soluble glycan chains by growing protoplasts (autoplasts) of Streptococcus faecalis.
Protoplasts (autoplasts) of Streptococcus faecalis were produced by the action of native autolytic N-acetylmuramidase in the absence of added peptidoglycan hydrolases and were grown in osmotically stabilized medium containing L-[3H]lysine and D-[14C]alanine. To reduce the level of muralytic hydrolysis of glycan chains during growth, heat-inactivated cell walls were added to the medium to bind autolytic enzyme, and tetracycline (1 mug/ml) was added to inhibit further enzyme synthesis. Under these conditions, protoplasts synthesized newly labeled peptidoglycan in the form of soluble, infrequently peptide cross-linked glycan chains which were released into the supernatant medium. These relatively large glycan chains were not transferred to exogenously added cell walls.
D000409:Alanine / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D013293:Enterococcus faecalis / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism*; D006868:Hydrolysis; D008239:Lysine / Q000378:metabolism; D009113:Muramidase / Q000378:metabolism; D010452:Peptide Biosynthesis; D010457:Peptidoglycan / Q000096:biosynthesis*; D011134:Polysaccharides / Q000096:biosynthesis*; D011523:Protoplasts / Q000378:metabolism*; D012995:Solubility; D013752:Tetracycline / Q000494:pharmacology
D010457:Peptidoglycan; D011134:Polysaccharides; D009113:Muramidase; D013752:Tetracycline; D008239:Lysine; D000409:Alanine