Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.
The D-alanine carboxypeptidase of B. subtilis is a membrane-bound enzyme which is inhibited by penicillins and binds them covalently. The enzyme has been labeled with [14C]- or [35S]penicillin. After tryptic or Pronase digestion of the labeled, denatured, reduced, and carboxymethylated enzyme, a radioactive peptide was isolated in each case. The amino acid compositions of these two peptides are reported. The Pronase peptide was a subset of the tryptic peptide. Neither contained a cysteine residue and the only amino acid in the Pronase peptide to which the penicillin could be bound was a serine residue.
D000409:Alanine; D001412:Bacillus subtilis / Q000201:enzymology; D001665:Binding Sites; D002268:Carboxypeptidases / Q000032:analysis / Q000378:metabolism*; D010400:Penicillin G / Q000378:metabolism*; D010455:Peptides / Q000302:isolation & purification* / Q000378:metabolism; D011402:Pronase; D014357:Trypsin
D010455:Peptides; D002268:Carboxypeptidases; D014357:Trypsin; D011402:Pronase; D000409:Alanine; D010400:Penicillin G