A Comparative Study of Claisen and Cope Rearrangements Catalyzed by Chorismate Mutase. An Insight into Enzymatic Efficiency: Transition State Stabilization or Substrate Preorganization?-Reference-Cited by-同舟云学术

A Comparative Study of Claisen and Cope Rearrangements Catalyzed by Chorismate Mutase. An Insight into Enzymatic Efficiency: Transition State Stabilization or Substrate Preorganization?

Published:2003-12-13 Issue:1 Volume:126 Page:311-319
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Martí Sergio¹,Andrés Juan¹,Moliner Vicente¹,Silla Estanislao¹,Tuñón Iñaki¹,Bertrán Juan¹

Affiliation:

1. Contribution from the Departament de Ciències Experimentals, Universitat Jaume I, Box 224, 12080 Castellón, Spain; Departament de Química Física/IcMol, Universitat de València, 46100 Burjassot, València, Spain; and Departament de Química, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0369156

Reference61 articles.

1. Haslam, E.Shikimic Acid: Metabolism and Metabolites; John Wiley & Sons: New York, 1993.

2. The mechanism of the chorismate mutase reaction

3. Monte Carlo Investigations of Solvent Effects on the Chorismate to Prephenate Rearrangement

4. Investigation of Solvent Effects for the Claisen Rearrangement of Chorismate to Prephenate: Mechanistic Interpretation via Near Attack Conformations

5. Conformational equilibrium of chorismate. A QM/MM theoretical study combining statistical simulations and geometry optimisations in gas phase and in aqueous solution

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