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. 1973 Jan;131(1):163-71.
doi: 10.1042/bj1310163.

Peptide inhibitors of Streptomyces DD-carboxypeptidases

M Nieto, H R Perkins, M Leyh-Bouille, J M Frère, J M Ghuysen

Peptide inhibitors of Streptomyces DD-carboxypeptidases

M Nieto et al. Biochem J. 1973 Jan.

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.

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