Peptide inhibitors of Streptomyces dd-carboxypeptidases
- 1 January 1973
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 131 (1), 163-171
- https://doi.org/10.1042/bj1310163
Abstract
1. Peptides that inhibit the dd-carboxypeptidases from Streptomyces strains albus G and R61 were synthesized. They are close analogues of the substrates of these enzymes. The enzymes from albus G and R61 strains are in general inhibited by the same peptides, but the enzyme from strain R39 differs considerably. 2. The two C-terminal residues of the peptide substrates and inhibitors appear to be mainly responsible for the initial binding of the substrate to the enzymes from albus G and R61 strains. The side chain in the third residue from the C-terminus seems critical in inducing catalytic activity. 3. Experimental evidence is presented suggesting that the amide bond linking the two C-terminal residues has a cis configuration when bound to the enzymes from strains albus G and R61. 4. The peptide inhibitors are not antibiotics against the same micro-organisms.Keywords
This publication has 13 references indexed in Scilit:
- Transpeptidase Activity of Streptomyces D-Alanyl-D CarboxypeptidasesProceedings of the National Academy of Sciences, 1972
- Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11Biochemistry, 1972
- Conformation of penicillin as a transition-state analog of the substrate of peptidoglycan transpeptidaseJournal of Molecular Biology, 1971
- Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61Biochemistry, 1971
- Substrate requirements of the Streptomyces albus G DD carboxypeptidaseBiochemistry, 1970
- Isolation of DD carboxypeptidase from Streptomyces albus G culture filtratesBiochemistry, 1970
- 2,6-Diamino-3-Hydroxypimelic Acid in Microbial Cell Wall MucopeptideNature, 1965
- 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
- Reaction of ninhydrin in acid solution with straight-chain amino acids containing two amino groups and its application to the estimation of α∈-diaminopimelic acidBiochemical Journal, 1957
- Energetics of Peptide FormationNature, 1952