Elucidation of Mechanism of Inhibition and X-ray Structure of the TEM-1 β-Lactamase from Escherichia coli Inhibited by a N-Sulfonyloxy-β-lactam-Reference-Cited by-同舟云学术

Elucidation of Mechanism of Inhibition and X-ray Structure of the TEM-1 β-Lactamase from Escherichia coli Inhibited by a N-Sulfonyloxy-β-lactam

Published:1999-05-27 Issue:23 Volume:121 Page:5353-5359
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Swarén Peter¹,Massova Irina¹,Bellettini John R.¹,Bulychev Alexey¹,Maveyraud Laurent¹,Kotra Lakshmi P.¹,Miller Marvin J.¹,Mobashery Shahriar¹,Samama Jean-Pierre¹

Affiliation:

1. Contribution from the Groupe de Cristallographie Biologique, Institut de Pharmacologie et de Biologie Structurale du CNRS, 205 route de Narbonne, 31077-Toulouse Cedex, France, Department of Chemistry, Wayne State University, Detroit, Michigan 48202, and Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja990400q

Reference19 articles.

1. Kinship and Diversification of Bacterial Penicillin-Binding Proteins and β-Lactamases

2. Evolution and Dissemination of β-Lactamases Accelerated by Generations of β-Lactam Antibiotics

3. Bush, K.; Mobashery, S. InResolving the Antibiotic Paradox: Progress inUnderstanding Drug Resistance and Development of New Antibiotics; Rosen, B. P., Mobashery, S., Eds.; Plenum Press: New York, 1998; pp 71−98.

4. A functional classification scheme for beta-lactamases and its correlation with molecular structure

5. Clinical isolates of Escherichia coli producing TRI β-lactamases: novel TEM-enzymes conferring resistance to β-lactamase inhibitors

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