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Antimicrobial Agents and Chemotherapy, August 2009, p. 3520-3523, Vol. 53, No. 8
0066-4804/09/$08.00+0 doi:10.1128/AAC.00219-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Laboratory of Bacteriology, Hellenic Pasteur Institute,1 Department of Microbiology, School of Medicine, University of Athens, Greece2
Received 17 February 2009/ Returned for modification 3 May 2009/ Accepted 17 May 2009
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 kcat values. Findings indicate a role of the
loop residue 211 in determining the substrate specificities of CMYs also corroborated by modeling studies.
Published ahead of print on 26 May 2009.
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