Inhibition of the Bacillus subtilis membrane-bound D-alanine carboxypeptidase by 6-aminopenicillanic acid covalently coupled to sepharose.
An insoluble penicillin derivative, 6-aminopenicillanic acid covalently coupled to Sepharose, was used to investigate the location of the d-alanine carboxypeptidase in the Bacillus subtilis membrane. Only 50% of the enzymatic activity in protoplasts and 74% of that in purified membranes was sensitive, although the purified enzyme could be inhibited completely by the resin. These results suggest that a minimum of 50% of the d-alanine carboxypeptidase exists on the outer face of the bacterial membrane.
D000409:Alanine; D001412:Bacillus subtilis / Q000201:enzymology*; D002250:Carbon Radioisotopes; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D002462:Cell Membrane / Q000201:enzymology; D055598:Chemical Phenomena; D002621:Chemistry; D002854:Chromatography, Paper; D010406:Penicillins / Q000494:pharmacology*; D011134:Polysaccharides / Q000494:pharmacology; D011523:Protoplasts / Q000201:enzymology; D013237:Stereoisomerism
D002250:Carbon Radioisotopes; D010406:Penicillins; D011134:Polysaccharides; D002268:Carboxypeptidases; D000409:Alanine