Three factors that modulate the activity of class D β-lactamases and interfere with the post-translational carboxylation of Lys70

0303 health sciences Protein Conformation Acylation Lysine Osmolar Concentration Crystallography, X-Ray Anti-Bacterial Agents 3. Good health Kinetics 03 medical and health sciences Amino Acid Substitution Bacterial Proteins Chlorides Catalytic Domain Pseudomonas aeruginosa Mutant Proteins Amino Acid Sequence Enzyme Inhibitors Hydrophobic and Hydrophilic Interactions Protein Processing, Post-Translational Conserved Sequence Moxalactam Protein Binding
DOI: 10.1042/bj20101122 Publication Date: 2010-11-26T11:08:26Z
ABSTRACT
The activity of class D β-lactamases is dependent on Lys70 carboxylation in the active site. Structural, kinetic and affinity studies show that this post-translational modification can be affected by the presence of a poor substrate such as moxalactam but also by the V117T substitution. Val117 is a strictly conserved hydrophobic residue located in the active site. In addition, inhibition of class D β-lactamases by chloride ions is due to a competition between the side chain carboxylate of the modified Lys70 and chloride ions. Determination of the individual kinetic constants shows that the deacylation of the acyl–enzyme is the rate-limiting step for the wild-type OXA-10 β-lactamase.
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