Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors.

@article{Perkins1973StreptomycesDA,
  title={Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors.},
  author={H. R. Perkins and Manuel Nieto and Jean Marie Fr{\`e}re and MELINA LEYH-BOUILLE and J. M. Ghuysen},
  journal={The Biochemical journal},
  year={1973},
  volume={131 4},
  pages={707-18}
}
The ability of the water-soluble dd-carboxypeptidases of Streptomyces strains albus G, R61, K11 and R39 to perform transpeptidation was studied. The donor was diacetyl-l-lysyl-d-alanyl-d-alanine, and a whole range of amino acids, peptides and structurally related amino compounds were tested for acceptor function. No compound tested was an acceptor for the enzyme from strain albus G whereas the enzymes from strains R61 and K11 could utilize with varying efficiency a wide range of substances… CONTINUE READING

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