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The roles of residues Tyr150, Glu272, and His314 in class C β‐lactamases by Dubus, Alain; Ledent, Philippe; Lamotte‐Brasseur, Josette; Frère, Jean‐Marie is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is The roles of residues Tyr150, Glu272, and His314 in class C β‐lactamases about?

Serine p-lactamases contribute widely to the p-lactam resistance phenomena. Unfortunately, the intimate details of their catalytic mechanism remain elusive and subject to some controversy even though many "natural" and "artificial" mutants of these different enzymes have been isolated. This paper is essentially focused on class C p-lactamases, which contain a Tyr (Tyr150) as the first residue of the second conserved element, in contrast to their class A counterparts, in which a Ser is found in the corresponding position. We have modified this Tyr residue by site-directed mutagenesis. On the basis of the three-dimensional structure of the Enterobacter cloacae P99 enzyme, it seemed that residues Glu272 and His314 might also be important. They were similarly substituted. The modified enzymes were isolated and their catalytic properties determined. Our results indicated that His314 was not required for catalysis and that Glu272 did not play an important role in acylation but was involved to a small extent in the deacylation process. Conversely, Tyrl50 was confirmed to be central for catalysis, at least with the best substrates. On the basis of a comparison of data obtained for several

Who reads The roles of residues Tyr150, Glu272, and His314 in class C β‐lactamases?

Author

Dubus, Alain; Ledent, Philippe; Lamotte‐Brasseur, Josette; Frère, Jean‐Marie

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

1996

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)