@article{1c16f84d2a384102b6181852f017deb9,
title = "Metallo-β-lactamase: Structure and mechanism",
abstract = "This past year has produced determinations of X-ray crystal structures for three metallo-β-lactamases and the elucidation of the catalytic mechanisms for a monozine and a dizinc enzyme. These advances shed light on how such a diverse group of enzymes are evolving to inactivate so efficiently a broad spectrum of β-lactam antibiotics.",
author = "Zhigang Wang and Walter Fast and Valentine, {Ann M.} and Benkovic, {Stephen J.}",
note = "Funding Information: Financial support for the work cited from the authors{\textquoteright} lab was provided by National Institutes of Health grant G.M. 56879-01 (to Stephen J Benkovic) and National Institutes of Health postdoctoral fellowships G.M. 18061 (to Zhigang Wang) and G.M. 20154 (to Ann M Valentine). We thank James Spencer at the Division of Protein Structure, National Institute of Medical Research, UK for providing us with the p rotein d ata b ank coordinates of the S. maltophilia metallo-β-lactamase crystal structure (1SML). ",
year = "1999",
month = oct,
day = "1",
doi = "10.1016/S1367-5931(99)00017-4",
language = "English (US)",
volume = "3",
pages = "614--622",
journal = "Current Opinion in Chemical Biology",
issn = "1367-5931",
publisher = "Elsevier Ltd",
number = "5",
}