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
AUTHORS (11)
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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CITATIONS (40)
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