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Preparation of Glutamate Analogues by Enzymatic Transamination

  • Thierry GefflautEmail author
  • Zeinab Assaf
  • Martine Sancelme
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 794)

Abstract

Aminotransferases are key enzymes of the metabolism of proteinogenic amino acids. These ubiquitous biocatalysts show high specific activities and relaxed substrate specificities making them valuable tools for the stereoselective synthesis of unnatural amino acids. We describe here the application of aspartate aminotransferase and branched chain aminotransferase from E. coli for the synthesis of various glutamate analogues, molecules of particular interest regarding the neuroactive properties of glutamic acid.

Key words

Glutamic acid Aminotransferase Transamination Stereoselective synthesis 

Notes

Acknowledgment

This work was supported by the French National Center for Scientific Research (CNRS). We are grateful to Kagamiyama’s group (Osaka Medical College) for providing us with the AspAT and BCAT overexpressing E. coli strains.

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Copyright information

© Springer Science+Business Media, LLC 2012

Authors and Affiliations

  • Thierry Gefflaut
    • 1
    Email author
  • Zeinab Assaf
    • 2
  • Martine Sancelme
    • 2
  1. 1.Lab SEESIBClermont Université, Université Blaise Pascal – CNRSAubièreFrance
  2. 2.Lab SEESIBClermont Université, Université Blaise PascalAubièreFrance

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