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A donor‐acceptor substrate of the exocellular DD‐carboxypeptidase‐transpeptidase from streptomyces R61
Author(s) -
Zeiger Allen R.,
Frére Jean-Marie,
Ghuysen Jean-Marie,
Perkins Harold R.
Publication year - 1975
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(75)80810-6
Subject(s) - library science , chemistry , humanities , philosophy , computer science
North-Holland Publishing Company Amsterdam of glycine of another hexapeptide, so that dimers or trimers (or rarely higher polymers) are built up [ 1 ] . The location of the physiological transpeptidase appears to be the plasma membrane [4]. An exocellular enzyme has been isolated from Streptomyces R6 1 and shown to have DD-carboxypeptidase and transpeptidase activities [ S-81. The enzyme was shown to catalyse the formation of a D-Ala-Gly peptide bond, such as is found in the native, completed wall peptidoglycan. An example of such a reaction is the transformation of Aca-LLys-D-Ala-D-Ala and Gly-LAla into Aca-LLys-D-Ala-Gly-L-Ala and D-alanine. In this report, it is shown that the tetrapeptide, p-[ l4 C] Ac-NE-(Gly)LLys-D-Ala-D-Ala, can serve as both donor and acceptor substrate of this enzyme, yielding several products, including one containing more than one D-Ala-Gly interpeptide linkage.