title: DD-peptidases and beta-lactamases: catalytic mechanisms and specificities.
abstract: DD-peptidases and beta-lactamases share several common properties, including the formation of an acylenzyme intermediate in their catalytic pathways. In their interactions with beta-lactam antibiotics, the stability of this intermediate is much higher with the peptidases than with the beta-lactamases. The structural factors responsible for this difference have not been identified. The evolution of beta-lactamases is taking place before our eyes, since mutants are constantly selected which can hydrolyze the molecules newly introduced as "beta-lactamase resistant" in the chemotherapeutic arsenal.
authors.affiliation: Laboratoire d'Enzymologie, Université de Liège, Sart Tilman, Belgium.
authors.forename: M
authors.initials: M
authors.lastname: Galleni
authors.forename: X
authors.initials: X
authors.lastname: Raquet
authors.forename: J
authors.initials: J
authors.lastname: Lamotte-Brasseur
authors.forename: E
authors.initials: E
authors.lastname: Fonzé
authors.forename: G
authors.initials: G
authors.lastname: Amicosante
authors.forename: J M
authors.initials: JM
authors.lastname: Frère
mesh_terms: D000595:Amino Acid Sequence; D002384:Catalysis; D008969:Molecular Sequence Data; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D011487:Protein Conformation; D013379:Substrate Specificity; D001618:beta-Lactamases / Q000378:metabolism*
chemical_list: D002267:Muramoylpentapeptide Carboxypeptidase; D001618:beta-Lactamases