| Preparation of glutamate analogues by enzymatic transamination. | |
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MedLine Citation:
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PMID: 21956556 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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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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Authors:
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Thierry Gefflaut; Zeinab Assaf; Martine Sancelme |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Methods in molecular biology (Clifton, N.J.) Volume: 794 ISSN: 1940-6029 ISO Abbreviation: Methods Mol. Biol. Publication Date: 2012 |
Date Detail:
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Created Date: 2011-09-29 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9214969 Medline TA: Methods Mol Biol Country: United States |
Other Details:
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Languages: eng Pagination: 55-72 Citation Subset: IM |
Affiliation:
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Lab SEESIB, Clermont Université, Université Blaise Pascal - CNRS, Aubière, France, Thierry.gefflaut@univ-bpclermont.fr. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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