Activity of three murein hydrolases during the cell division cycle of Escherichia coli K-12 as measured in toluene-treated cells.
The specific activities of three murein hydrolases, carboxypeptidase I, carboxypeptidase II, and amidase were studied with respect to cell division in toluene-treated cells of Escherichia coli K-12. Carboxypeptidase I and amidase activities were constant throughout the division cycle in cells of D11/lac+pro+. Detectable carboxypeptidase II activity varied and was highest at the time of division by a factor of three. Carboxypeptidase II specific activity was also correlated with cell division in BUG 6, a temperature-sensitive mutant (J.N Reeve, D.J. Groves, and D.J. Clark, 1970). Fifteen minutes after shifting BUG 6 from 42 C (nondividing conditions) to 32 C (dividing conditions), there was a rapid resumption of cell division, accompanied by a 10-fold increase in the specific activity of carboxypeptidase II. These results demonstrate a correlation between detectable carboxypeptidase II activity and cell division as reflected by activity in toluene-treated cells. The subcellular location of carboxypeptidase II, a soluble enzyme was found to be periplasmic since it was released by tris(hydroxymethyl)-aminomethane-ethylenediaminetetraacetate treatment and osmotic shock, two methods known to release periplasmic enzymes.
D000581:Amidohydrolases / Q000378:metabolism*; D002268:Carboxypeptidases / Q000378:metabolism*; D002455:Cell Division; D002474:Cell-Free System; D003593:Cytoplasm / Q000201:enzymology; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology / Q000254:growth & development*; D005696:Galactosidases / Q000378:metabolism; D006868:Hydrolysis; D009154:Mutation; D010457:Peptidoglycan / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology; D013696:Temperature; D014050:Toluene / Q000494:pharmacology
D010457:Peptidoglycan; D014050:Toluene; D005696:Galactosidases; D002268:Carboxypeptidases; D000581:Amidohydrolases