QM/MM Studies of Monozinc β-Lactamase CphA Suggest That the Crystal Structure of an Enzyme−Intermediate Complex Represents a Minor Pathway
- 7 December 2010
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 132 (51), 17986-17988
- https://doi.org/10.1021/ja104241g
Abstract
QM/MM studies of the hydrolysis of a β-lactam antibiotic molecule (biapenem) catalyzed by a monozinc β-lactamase (CphA) have revealed the complete reaction mechanism and shown that an experimentally determined enzyme−intermediate complex is a stable intermediate or product in a minor pathway.Keywords
This publication has 31 references indexed in Scilit:
- Catalytic Role of the Metal Ion in the Metallo-β-lactamase GOBJournal of Biological Chemistry, 2010
- Evolving Carbapenemases: Can Medicinal Chemists Advance One Step Ahead of the Coming Storm?Journal of Medicinal Chemistry, 2010
- Common Mechanistic Features among Metallo-β-lactamasesPublished by Elsevier BV ,2009
- Adaptive protein evolution grants organismal fitness by improving catalysis and flexibilityProceedings of the National Academy of Sciences of the United States of America, 2008
- Trapping and Characterization of a Reaction Intermediate in Carbapenem Hydrolysis by B. cereus Metallo-β-lactamaseJournal of the American Chemical Society, 2008
- Role of the Zn1and Zn2sites in Metallo-β-lactamase L1Journal of the American Chemical Society, 2008
- Mechanistic Studies on the Mononuclear ZnII-Containing Metallo-β-lactamase ImiS from Aeromonas sobriaBiochemistry, 2006
- A Metallo-β-lactamase Enzyme in Action: Crystal Structures of the Monozinc Carbapenemase CphA and its Complex with BiapenemJournal of Molecular Biology, 2005
- All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of ProteinsThe Journal of Physical Chemistry B, 1998
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983