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.
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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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Gefflaut, T., Assaf, Z., Sancelme, M. (2012). Preparation of Glutamate Analogues by Enzymatic Transamination. In: Pollegioni, L., Servi, S. (eds) Unnatural Amino Acids. Methods in Molecular Biology, vol 794. Humana Press. https://doi.org/10.1007/978-1-61779-331-8_4
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DOI: https://doi.org/10.1007/978-1-61779-331-8_4
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