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Synthetic peptide inhibitors of transpeptidation by the exocellular DD‐carboxypeptidase‐transpeptidase from Actinomadura R39
Author(s) -
Perkins Harold R.,
Frère Jean-Marie,
Ghuysen Jean-Marie
Publication year - 1981
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(81)80023-3
Subject(s) - library science , computer science
The penicillin-sensitive exocellular carboxypeptidases-transpeptidases of Actinomycetes have been extensively studied as models of peptidoglycan construction and modification in relation to their mode of enzyme action and their mechanism of inhibition by fl-lactam antibiotics [ 1,2]. The enzyme from Actinomadura R39 has been purified to homogeneity [3] and is known to catalyse hydrolysis of the C-terminal D-alanyl-D-alanine peptide bound in natural and synthetic substrates (e.g., Acz-L-Lys-D-AlaD-Ala) or, in the presence of a suitable acceptor, to perform transpeptidation in which an acceptor moiety such as meso-diaminopimelic acid (A, pm) replaces the terminal D-alanine [4]. The amount of transpeptidation relative to carboxypeptidase action in a particular digest was highly sensitive to the concentration of a ‘natural’ acceptor: