Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis. | Zendy

N H Georgopapadakou | Zendy; Sven Hammarström | Zendy; Jack L. Strominger | Zendy

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Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.

Author(s) -

N H Georgopapadakou,

Sven Hammarström,

Jack L. Strominger

Publication year - 1977

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.74.3.1009

Subject(s) - pronase , peptide , bacillus subtilis , biochemistry , carboxypeptidase , residue (chemistry) , alanine , chemistry , enzyme , serine , amino acid , peptide sequence , papain , cysteine , trypsin , biology , bacteria , gene , genetics

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.

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