Abstract
Site-directed mutagenesis of CphA indicated that prolines in the P158-P172 loop are essential for the stability and the catalytic activity of subclass B2 metallo-β-lactamases against carbapenems. The sequential substitution of proline led to a decrease of the catalytic efficiency of the variant compared to the wild-type (WT) enzyme but also to a higher affinity for the binding of the second zinc ion.
Copyright © 2016, American Society for Microbiology. All Rights Reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Binding Sites
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Carbapenems / pharmacology*
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Kinetics
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Proline / chemistry
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Proline / metabolism
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Sequence Analysis, Protein
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Structure-Activity Relationship
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Substrate Specificity / genetics
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Substrate Specificity / physiology
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Zinc / pharmacology
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beta-Lactamases / chemistry
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beta-Lactamases / genetics
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beta-Lactamases / metabolism*
Substances
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Bacterial Proteins
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Carbapenems
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Proline
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beta-Lactamases
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Zinc