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. 1991 Dec 1;280(Pt 2):499–506. doi: 10.1042/bj2800499

Accumulation of acyl-enzyme in DD-peptidase-catalysed reactions with analogues of peptide substrates.

M Jamin 1, M Adam 1, C Damblon 1, L Christiaens 1, J M Frère 1
PMCID: PMC1130576  PMID: 1747125

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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