On the Ionization State of the Substrate in the Active Site of Glutamate Racemase. A QM/MM Study about the Importance of Being Zwitterionic-Reference-Cited by-同舟云学术

On the Ionization State of the Substrate in the Active Site of Glutamate Racemase. A QM/MM Study about the Importance of Being Zwitterionic

Published:2005-11-25 Issue:2 Volume:110 Page:717-725
ISSN:1089-5639
Container-title:The Journal of Physical Chemistry A
language:en
Short-container-title:J. Phys. Chem. A

Author:

Puig Eduard¹,Garcia-Viloca Mireia¹,González-Lafont Àngels¹,Lluch José M.¹

Affiliation:

1. Departament de Química, Universitat Autònoma de Barcelona, Bellaterra (Barcelona), Spain, and Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra (Barcelona), Spain

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp054555y

Reference45 articles.

1. Understanding Nature's Strategies for Enzyme-Catalyzed Racemization and Epimerization

2. Enzymatic Racemisation and its Application to Synthetic Biotransformations

3. Amino acid racemases: Functions and mechanisms

4. Regulation of the Glutamate Racemase ofEscherichia coliInvestigated by Site-Directed Mutagenesis

5. 4-Substituted d-Glutamic Acid Analogues: The First Potent Inhibitors of Glutamate Racemase (MurI) Enzyme with Antibacterial Activity

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