Critical Role of Tryptophan 154 for the Activity and Stability of Class D β-Lactamases,-Reference-Cited by-同舟云学术

Critical Role of Tryptophan 154 for the Activity and Stability of Class D β-Lactamases,

Published:2009-11-05 Issue:47 Volume:48 Page:11252-11263
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Baurin Stéphane¹,Vercheval Lionel¹,Bouillenne Fabrice²,Falzone Claudia³,Brans Alain²,Jacquamet Lilian⁴,Ferrer Jean-Luc⁴,Sauvage Eric³,Dehareng Dominique²,Frère Jean-Marie²,Charlier Paulette³,Galleni Moreno¹,Kerff Frédéric³

Affiliation:

1. Laboratory of Biological Macromolecules

2. Laboratory of Enzymology

3. Laboratory of Protein Crystallography, Center for Protein Engineering

4. Laboratoire de Crystallographie et Crystallogenèse des Protéines, Institut de Biologie Structurale J.-P. Ebel, CEA/CNRS/UJ.F, 38027 Grenoble Cedex 1, France.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi901548c

Reference50 articles.

1. The β-lactamase cycle: a tale of selective pressure and bacterial ingenuity

2. The structure of β-lactamases

3. ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type.

4. Sequence of the OXA2 β-lactamase: comparison with other penicillin-reactive enzymes

5. Three-Dimensional Structure of AmpC β-Lactamase from Escherichia coli Bound to a Transition-State Analogue: Possible Implications for the Oxyanion Hypothesis and for Inhibitor Design

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