title: Extended-spectrum properties of CMY-30, a Val211Gly mutant of CMY-2 cephalosporinase.
abstract: CMY-30, a Val211Gly mutant of CMY-2 cephalosporinase, was derived by mutagenesis. The hydrolytic efficiency of CMY-30 against expanded-spectrum cephalosporins was higher than that of CMY-2 due to increased k(cat) values. Findings indicate a role of the Omega loop residue 211 in determining the substrate specificities of CMYs also corroborated by modeling studies.
authors.affiliation: Laboratory of Bacteriology, Hellenic Pasteur Institute, Vas. Sofias 127, Athens 11521, Greece.
authors.forename: Stathis D
authors.initials: SD
authors.lastname: Kotsakis
authors.forename: Costas C
authors.initials: CC
authors.lastname: Papagiannitsis
authors.forename: Eva
authors.initials: E
authors.lastname: Tzelepi
authors.forename: Leonidas S
authors.initials: LS
authors.lastname: Tzouvelekis
authors.forename: Vivi
authors.initials: V
authors.lastname: Miriagou
mesh_terms: D001398:Aztreonam / Q000378:metabolism; D002442:Ceftazidime / Q000378:metabolism; D002511:Cephalosporins / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D001618:beta-Lactamases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D047090:beta-Lactams / Q000378:metabolism
chemical_list: D002511:Cephalosporins; D029968:Escherichia coli Proteins; D047090:beta-Lactams; D002442:Ceftazidime; C103022:beta-lactamase CMY-2; D001618:beta-Lactamases; D001398:Aztreonam