Crystal Structure of 6α-(Hydroxymethyl)penicillanate Complexed to the TEM-1 β-Lactamase from Escherichia coli: Evidence on the Mechanism of Action of a Novel Inhibitor Designed by a Computer-Aided Process-Reference-Cited by-同舟云学术

Crystal Structure of 6α-(Hydroxymethyl)penicillanate Complexed to the TEM-1 β-Lactamase from Escherichia coli: Evidence on the Mechanism of Action of a Novel Inhibitor Designed by a Computer-Aided Process

Published:1996-01-01 Issue:32 Volume:118 Page:7435-7440
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Maveyraud Laurent¹,Massova Irina¹,Birck Catherine¹,Miyashita Kazuyuki¹,Samama Jean-Pierre¹,Mobashery Shahriar¹

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, and Department of Chemistry, Wayne State University, Detroit, Michigan 48202-3489

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9609718

Reference16 articles.

1. Design, Synthesis, and Evaluation of a Potent Mechanism-Based Inhibitor for the TEM .beta.-Lactamase with Implications for the Enzyme Mechanism

2. Penem BRL 42715: An Effective Inactivator for .beta.-Lactamases

3. Potent mechanism-based inhibition of the TEM-1 .beta.-lactamase by novel N-sulfonyloxy .beta.-lactams

4. Crystallization and preliminary crystallographic data on Escherichia coli TEM1 β-lactamase

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