Document Detail


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