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
- 1 January 1996
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 118 (32) , 7435-7440
- https://doi.org/10.1021/ja9609718
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Inhibition of β-lactamase by clavulanate: Trapped intermediates in cryocrystallographic studiesPublished by Elsevier ,2004
- Design, Synthesis, and Evaluation of a Potent Mechanism-Based Inhibitor for the TEM .beta.-Lactamase with Implications for the Enzyme MechanismJournal of the American Chemical Society, 1995
- Electrostatic analysis of TEM1 β-lactamase: effect of substrate binding, steep potential gradients and consequences of site-directed mutationsStructure, 1995
- Potent mechanism-based inhibition of the TEM-1 .beta.-lactamase by novel N-sulfonyloxy .beta.-lactamsJournal of the American Chemical Society, 1995
- Penem BRL 42715: An Effective Inactivator for .beta.-LactamasesJournal of the American Chemical Society, 1995
- Assessment of bulk solvent models by cross-validationActa Crystallographica Section A Foundations of Crystallography, 1993
- Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolutionNature, 1992
- Elucidation of the role of arginine-224 in the turnover processes of class A .beta.-lactamasesBiochemistry, 1992
- Crystallization and preliminary crystallographic data on Escherichia coli TEM1 β-lactamaseJournal of Molecular Biology, 1992
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991