Understanding the Role of Active‐Site Residues in Chorismate Mutase Catalysis from Molecular‐Dynamics Simulations
- 4 April 2003
- journal article
- review article
- Published by Wiley in Angewandte Chemie International Edition in English
- Vol. 42 (13) , 1508-1511
- https://doi.org/10.1002/anie.200219878
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- A QM/MM Implementation of the Self-Consistent Charge Density Functional Tight Binding (SCC-DFTB) MethodThe Journal of Physical Chemistry B, 2000
- All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of ProteinsThe Journal of Physical Chemistry B, 1998
- Simulation of activation free energies in molecular systemsThe Journal of Chemical Physics, 1996
- Der Mechanismus der Claisen‐Umlagerung – ein Déjà‐vuAngewandte Chemie, 1996
- The mechanism of the catalysis of the Claisen rearrangement of chorismate to prephenate by the chorismate mutase from Bacillus subtilis. A molecular mechanics and hybrid quantum mechanical/molecular mechanical studyJournal of the Chemical Society, Perkin Transactions 2, 1996
- Insights into Chorismate Mutase Catalysis from a Combined QM/MM Simulation of the Enzyme ReactionJournal of the American Chemical Society, 1995
- The Monofunctional Chorismate Mutase from Bacillus subtilisJournal of Molecular Biology, 1994
- Monofunctional chorismate mutase from Bacillus subtilis: kinetic and carbon-13 NMR studies on the interactions of the enzyme with its ligandsBiochemistry, 1990
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Monte Carlo free energy estimates using non-Boltzmann sampling: Application to the sub-critical Lennard-Jones fluidChemical Physics Letters, 1974