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. 1991 Sep 15;278(Pt 3):673–678. doi: 10.1042/bj2780673

The mutation Lys234His yields a class A beta-lactamase with a novel pH-dependence.

J Brannigan 1, A Matagne 1, F Jacob 1, C Damblon 1, B Joris 1, D Klein 1, B G Spratt 1, J M Frère 1
PMCID: PMC1151399  PMID: 1910335

Abstract

The lysine-234 residue is highly conserved in beta-lactamases and in nearly all active-site-serine penicillin-recognizing enzymes. Its replacement by a histidine residue in the Streptomyces albus G class A beta-lactamase yielded an enzyme the pH-dependence of which was characterized by the appearance of a novel pK, which could be attributed to the newly introduced residue. At low pH, the kcat, value for benzylpenicillin was as high as 50% of that of the wild-type enzyme, demonstrating that an efficient active site was maintained. Both kcat. and kcat/Km dramatically decreased above pH 6 but the decrease in kcat./Km could not be attributed to larger Km values. Thus a positive charge on the side chain of residue 234 appears to be more essential for transition-state stabilization than for initial recognition of the substrate ground state.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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