Thioester substrates can be used to study the hydrolysis and transfer reactions catalysed by beta-lactamases and DD-peptidases. With the latter enzymes, accumulation of the acyl-enzyme can be detected directly. The efficiency of various amines as acceptor substrates was in excellent agreement with previous results obtained with peptide substrates of the DD-peptidases. The results indicated the presence of a specific binding site for the acceptor substrates. Although most of the results agreed well with a simple partition model, more elaborate hypotheses will be needed to account for all the data presented.
Accumulation of acyl-enzyme in dd-peptidase-catalysed reactions with analogues of peptide substrates
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M Jamin, M Adam, C Damblon, L Christiaens, J M Frère; Accumulation of acyl-enzyme in dd-peptidase-catalysed reactions with analogues of peptide substrates. Biochem J 1 December 1991; 280 (2): 499–506. doi: https://doi.org/10.1042/bj2800499
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