Extended-spectrum properties of CMY-30, a Val211Gly mutant of CMY-2 cephalosporinase.
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.
Kotsakis
Stathis D
SD
Laboratory of Bacteriology, Hellenic Pasteur Institute, Vas. Sofias 127, Athens 11521, Greece.
Papagiannitsis
Costas C
CC
Tzelepi
Eva
E
Tzouvelekis
Leonidas S
LS
Miriagou
Vivi
V
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
D002511:Cephalosporins; D029968:Escherichia coli Proteins; D047090:beta-Lactams; D002442:Ceftazidime; C103022:beta-lactamase CMY-2; D001618:beta-Lactamases; D001398:Aztreonam