Effects of sulfhydryl reagents on the binding and release of penicillin G by D-alanine carboxypeptidase IA of Escherichia coli.
Open Access
- 1 April 1978
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 253 (8), 2584-2588
- https://doi.org/10.1016/s0021-9258(17)40861-1
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- Utilization of a depsipeptide substrate for trapping acyl—enzyme intermediates of penicillin-sensitive D-alanine carboxypeptidasesProceedings of the National Academy of Sciences, 1978
- Simultaneous deletion of D-alanine carboxypeptidase IB-C and penicillin-binding component IV in a mutant of Escherichia coli K12.Proceedings of the National Academy of Sciences, 1977
- Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity.Proceedings of the National Academy of Sciences, 1977
- Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.Proceedings of the National Academy of Sciences, 1977
- Properties of the Penicillin‐Binding Proteins of Escherichia coli K12European Journal of Biochemistry, 1977
- A possible role for a single cysteine residue in carboxypeptidase YFEBS Letters, 1975
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973
- Isolation by Covalent Affinity Chromatography of the Penicillin-Binding Components from Membranes of Bacillus subtilisProceedings of the National Academy of Sciences, 1972
- Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine.Proceedings of the National Academy of Sciences, 1965
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951