Murein structure and lack of DD- and LD-carboxypeptidase activities in Caulobacter crescentus.
High-pressure liquid chromatography of a muramidase digest of murein sacculi from Caulobacter crescentus showed that the absence of D-alanine carboxypeptidase activity in the cells was reflected by a very high content of pentapeptide in the murein. Approximately half of the pentapeptide side chains were shown to contain glycine, which replaced D-alanine as the terminal amino acid.
D000596:Amino Acids / Q000032:analysis; D001419:Bacteria / Q000201:enzymology*; D002268:Carboxypeptidases / Q000235:genetics*; D002851:Chromatography, High Pressure Liquid; D009113:Muramidase; D002267:Muramoylpentapeptide Carboxypeptidase / Q000235:genetics*; D010457:Peptidoglycan / Q000096:biosynthesis / Q000302:isolation & purification*
D000596:Amino Acids; D010457:Peptidoglycan; D009113:Muramidase; D002268:Carboxypeptidases; C021505:LD-carboxypeptidase; D002267:Muramoylpentapeptide Carboxypeptidase