Characterization of autolysins from Mycobacterium smegmatis.
This study demonstrates, for the first time, the autolytic enzymes associated with mycobacterial cell walls. Based on the release of radioactivity and ninhydrin-reactive material from isolated cell walls, it was shown that maximum activity occurs during the late log phase of growth and at a buffer pH of about 8.0. Chemical analyses of autolytic digests of isolated cell walls indicated that at least three autolysins are active under the conditions used. These are N-glycolylmuramic acid-L-alanine amidase, an aminopeptidase that releases L-alanine, and an endopeptidase that solubilizes and L-alanyl-D-glutamic acid dippetide. No other endopeptidase, carboxypeptidase, or glycosidase activity was detected.
D000409:Alanine / Q000032:analysis; D000581:Amidohydrolases / Q000378:metabolism*; D000626:Aminopeptidases / Q000378:metabolism*; D002473:Cell Wall / Q000032:analysis / Q000378:metabolism; D003960:Diaminopimelic Acid / Q000032:analysis; D010450:Endopeptidases / Q000378:metabolism*; D005971:Glutamates / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D009161:Mycobacterium / Q000032:analysis / Q000201:enzymology* / Q000378:metabolism; D012995:Solubility
D005971:Glutamates; D003960:Diaminopimelic Acid; D010450:Endopeptidases; D000626:Aminopeptidases; D000581:Amidohydrolases; D000409:Alanine