Abstract
β-Lactamase inhibitory protein II (BLIP-II) is a potent inhibitor of class A β-lactamases. KPC-2 is a class A β-lactamase that is capable of hydrolyzing carbapenems and has become a widespread source of resistance to these drugs for Gram-negative bacteria. Determination of association and dissociation rate constants for binding between BLIP-II and KPC-2 reveals a very tight interaction with a calculated (koff/kon) equilibrium dissociation constant of 76 fM (76 × 10(-15) M).
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Bacterial Proteins / antagonists & inhibitors*
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Bacterial Proteins / metabolism*
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Carbapenems / metabolism
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Klebsiella pneumoniae / drug effects*
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Klebsiella pneumoniae / enzymology*
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Microbial Sensitivity Tests
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beta-Lactamase Inhibitors*
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beta-Lactamases
Substances
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Bacterial Proteins
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Carbapenems
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beta-Lactamase Inhibitors
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beta-lactamase-inhibitor protein, Streptomyces
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beta-Lactamases
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carbapenemase-2, Klebsiella pneumoniae