Reaction Mechanism of the Mandelate Anion Racemization Catalyzed by Mandelate Racemase Enzyme: A QM/MM Molecular Dynamics Free Energy Study
Author:
Affiliation:
1. Departament de Química, Universitat Autònoma de Barcelona, 08193 Bellaterra (Barcelona), Spain, and Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, 08193 Bellaterra (Barcelona), Spain
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp052239d
Reference62 articles.
1. Mandelate Racemase: Structure-Function Studies of a Pseudosymmetric Enzyme
2. Electrophilic catalysis can explain the unexpected acidity of carbon acids in enzyme-catalyzed reactions
3. Mechanism of the Reaction Catalyzed by Mandelate Racemase: Importance of Electrophilic Catalysis by Glutamic Acid 317
4. Mandelate Racemase in Pieces: Effective Concentrations of Enzyme Functional Groups in the Transition State
5. Hydrophobic Nature of the Active Site of Mandelate Racemase
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3. Molecular dynamics perspective on the thermal stability of mandelate racemase;Journal of Biomolecular Structure and Dynamics;2018-01-25
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