A Pseudomonas aeruginosa isolate recovered in Belgium produced a novel extended-spectrum ß-lactamase, BEL-2, differing from BEL-1 by a single Leu162Phe substitution. That modification significantly altered the kinetic properties of the enzyme, increasing its affinity for expanded-spectrum cephalosporins. The blaBEL-2 gene was identified from a P. aeruginosa isolate clonally related to another blaBEL-1-positive isolate. Copyright © 2010, American Society for Microbiology. All Rights Reserved.
Poirel, L., Docquier, J.D., DE LUCA, F., Verlinde, A., Ide, L., Rossolini, G.M., et al. (2010). BEL-2, an extended-spectrum beta-lactamase with increased activity toward expanded-spectrum cephalosporins in Pseudomonas aeruginosa. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 54(1), 533-535 [10.1128/AAC.00859-09].
BEL-2, an extended-spectrum beta-lactamase with increased activity toward expanded-spectrum cephalosporins in Pseudomonas aeruginosa
DOCQUIER J. D.;
2010-01-01
Abstract
A Pseudomonas aeruginosa isolate recovered in Belgium produced a novel extended-spectrum ß-lactamase, BEL-2, differing from BEL-1 by a single Leu162Phe substitution. That modification significantly altered the kinetic properties of the enzyme, increasing its affinity for expanded-spectrum cephalosporins. The blaBEL-2 gene was identified from a P. aeruginosa isolate clonally related to another blaBEL-1-positive isolate. Copyright © 2010, American Society for Microbiology. All Rights Reserved.
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https://hdl.handle.net/11365/2877
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