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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Aztreonam / metabolism
-
Ceftazidime / metabolism
-
Cephalosporins / metabolism*
-
Escherichia coli Proteins / chemistry
-
Escherichia coli Proteins / genetics*
-
Escherichia coli Proteins / metabolism
-
Protein Binding
-
Protein Structure, Secondary
-
beta-Lactamases* / chemistry
-
beta-Lactamases* / genetics
-
beta-Lactamases* / metabolism
-
beta-Lactams / metabolism
Substances
-
Cephalosporins
-
Escherichia coli Proteins
-
beta-Lactams
-
Ceftazidime
-
beta-lactamase CMY-2
-
beta-Lactamases
-
Aztreonam