Murein hydrolases of Caulobacter crescentus.
Caulobacter crescentus was found to exhibit a similar autolytic response to a variety of factors affecting the structure of the cell envelope and interfering with murein synthesis as several other species of bacteria. Autolysis was accompanied by the hydrolysis of murein with the release of soluble degradation products. Several murein hydrolases with different bond specificity were found and except for the absence of DD-carboxypeptidase and LD-carboxypeptidase activities the make-up of these enzymes resembled that of the well studied bacterium Escherichia coli.
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Markiewicz
D000581:Amidohydrolases / Q000032:analysis / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D001433:Bacteriolysis; D001455:Bambermycins / Q000494:pharmacology; D002268:Carboxypeptidases / Q000032:analysis; D002462:Cell Membrane / Q000201:enzymology; D008274:Magnesium / Q000494:pharmacology; D002267:Muramoylpentapeptide Carboxypeptidase / Q000032:analysis; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism*; D013045:Species Specificity
D010457:Peptidoglycan; D001455:Bambermycins; D002268:Carboxypeptidases; D002267:Muramoylpentapeptide Carboxypeptidase; D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase; D008274:Magnesium