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PMID: 403523 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 3 ·1977-03-00 ·Pages 1009-12

Georgopapadakou N, Hammarström S, Strominger JL

Abstract

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.

MeSH Terms
Alanine Bacillus subtilis/enzymology Binding Sites Carboxypeptidases/analysis,metabolism Penicillin G/metabolism Peptides/isolation & purification,metabolism Pronase Trypsin
Chemicals
Peptides Carboxypeptidases Trypsin Pronase Alanine Penicillin G
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Georgopapadakou N
Hammarström S
Strominger J L
References (19)
19 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.74.3.1009
Published
1977-03-00
Pages
1009-12
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC430565
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.74.3.1009 PMC Full Text View journal details
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