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PMID: 10508665 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Metallo-beta-lactamase: structure and mechanism.

Current opinion in chemical biology ·Vol. 3 ·No. 5 ·1999-10-00 ·Pages 614-22

Wang Z, Fast W, Valentine AM, Benkovic SJ

Abstract

This past year has produced determinations of X-ray crystal structures for three metallo-beta-lactamases and the elucidation of the catalytic mechanisms for a monozinc 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 beta-lactam antibiotics.

MeSH Terms
Amino Acid Sequence Catalysis Models, Molecular Molecular Sequence Data Protein Conformation Sequence Alignment Structure-Activity Relationship beta-Lactamases/chemistry,metabolism
Chemicals
beta-Lactamases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Wang Z
The Pennsylvania State University, Department of Chemistry, 152 Davey Laboratory, University Park, PA 16802, USA.
Fast W
Valentine A M
Benkovic S J
Article Info
Journal
Current opinion in chemical biology
Abbr.
Curr Opin Chem Biol
ISSN
1367-5931
DOI
10.1016/s1367-5931(99)00017-4
Published
1999-10-00
Pages
614-22
Language
English
Region
England
NLM ID
9811312
Subset
IM
Grants
NIGMS NIH HHS · GM 18061 · United States
NIGMS NIH HHS · GM 20154 · United States
NIGMS NIH HHS · GM 56879-01 · United States
External Links
PubMed source DOI: 10.1016/s1367-5931(99)00017-4 View journal details
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