Carbon-13 NMR studies of the enzyme-product complex of Bacillus subtilis chorismate mutase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00066a017
Reference43 articles.
1. Secondary tritium isotope effects as probes of the enzymic and nonenzymic conversion of chorismate to prephenate
2. [19] Carbon-13 nuclear magnetic resonance: New techniques
3. Rearrangement of chorismate to prephenate. Use of chorismate mutase inhibitors to define the transition state structure
4. Molecular Orbital Studies of Enzyme Catalysed Reactions. Rearrangement of Chorismate to Prephenate
5. Transition-state stabilization and enzymic catalysis. Kinetic and molecular orbital studies of the rearrangement of chorismate to prephenate
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1. Investigation of Ligand Binding and Protein Dynamics in Bacillus subtilis Chorismate Mutase by Transverse Relaxation Optimized Spectroscopy−Nuclear Magnetic Resonance,;Biochemistry;2005-04-15
2. Comparison of Formation of Reactive Conformers (NACs) for the Claisen Rearrangement of Chorismate to Prephenate in Water and in the E. coli Mutase: The Efficiency of the Enzyme Catalysis;Journal of the American Chemical Society;2003-04-19
3. Direct NMR observation and DFT calculations of a hydrogen bond at the active site of a 44 kDa enzyme;Journal of Biomolecular NMR;2002
4. An MD/QM Study of the Chorismate Mutase-Catalyzed Claisen Rearrangement Reaction;The Journal of Physical Chemistry B;2001-06-19
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