title: Biochemical characterization of the metallo-beta-lactamase CcrA from Bacteroides fragilis TAL3636.
abstract: The CcrA beta-lactamase from Bacteroides fragilis TAL3636 was cloned into Escherichia coli and purified from inclusion bodies. This group 3 metalloenzyme hydrolyzed most beta-lactam antibiotics, including cephamycins and carbapenems. Following inhibition by chelators, enzyme activity was recovered with the cations Zn2+ and Co2+. Clavulanate and sulbactam were activators; tazobactam at 10 microM inactivated the enzyme.
authors.affiliation: Medical Research Division, American Cyanamid Corporation, Pearl River, New York 10965.
authors.forename: Y
authors.initials: Y
authors.lastname: Yang
authors.forename: B A
authors.initials: BA
authors.lastname: Rasmussen
authors.forename: K
authors.initials: K
authors.lastname: Bush
mesh_terms: D001441:Bacteroides fragilis / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D001618:beta-Lactamases / Q000032:analysis*
chemical_list: D001618:beta-Lactamases