[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
JAMIN, M.
Adam, Maggy
Damblon, Christian ; Université de Liège - ULiège > Département de chimie (sciences) > Chimie biologique structurale
Christiaens, Léon ; Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences)
Frère, Jean-Marie ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Language :
English
Title :
ACCUMULATION OF ACYL-ENZYME IN DD-PEPTIDASE-CATALYZED REACTIONS WITH ANALOGS OF PEPTIDE-SUBSTRATES