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ACCUMULATION OF ACYL-ENZYME IN DD-PEPTIDASE-CATALYZED REACTIONS WITH ANALOGS OF PEPTIDE-SUBSTRATES
JAMIN, M.; Adam, Maggy; Damblon, Christian et al.
1991In Biochemical Journal, 280 (Part 2), p. 499-506
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Abstract :
[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
Publication date :
1991
Journal title :
Biochemical Journal
ISSN :
0264-6021
eISSN :
1470-8728
Publisher :
Portland Press, London, United Kingdom
Volume :
280
Issue :
Part 2
Pages :
499-506
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 27 November 2010

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