title: Accumulation of acyl-enzyme in DD-peptidase-catalysed reactions with analogues of peptide substrates.
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.
authors.affiliation: Laboratoire d'Enzymologie, Université de Liège, Belgium.
authors.forename: M
authors.initials: M
authors.lastname: Jamin
authors.forename: M
authors.initials: M
authors.lastname: Adam
authors.forename: C
authors.initials: C
authors.lastname: Damblon
authors.forename: L
authors.initials: L
authors.lastname: Christiaens
authors.forename: J M
authors.initials: JM
authors.lastname: Frère
mesh_terms: D000215:Acylation; D000438:Alcohols / Q000378:metabolism; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D002384:Catalysis; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity; D001618:beta-Lactamases / Q000378:metabolism
chemical_list: D000438:Alcohols; D000596:Amino Acids; D002267:Muramoylpentapeptide Carboxypeptidase; D001618:beta-Lactamases