Application of aminoacylase I to the enantioselective resolution of α-amino acid esters and amides
| Autor: | Roger A. Sheldon, M. I. Youshko, Luuk M. van Langen, Vytas K. Švedas |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
chemistry.chemical_classification
Resolution (mass spectrometry) Stereochemistry Organic Chemistry Aminoacylase I Enantioselective synthesis Catalysis Amino acid Inorganic Chemistry Hydrolysis chemistry.chemical_compound Enzyme Enantiopure drug chemistry Amide Organic chemistry Physical and Theoretical Chemistry |
| Zdroj: | Tetrahedron: Asymmetry. 15:1933-1936 |
| ISSN: | 0957-4166 |
| DOI: | 10.1016/j.tetasy.2004.05.018 |
| Popis: | Aminoacylase I from Aspergillus melleus , a readily available and inexpensive enzyme mainly used in the industrial production of enantiopure l -amino acids from their N -acetyl derivatives, is shown to hydrolyze the esters and amides of natural and non-natural amino acids with high enantioselectivity (for the ester hydrolysis, E is up to 76, in case of amides E >300). The reaction rates of amide and ester hydrolysis are comparable, and in some cases these conversions proceeded even faster than `traditional' aminoacylase-catalyzed hydrolysis of N -acetyl derivatives thus providing new possibilities for the resolution of the corresponding racemates. This novel approach provides an alternative route for the biocatalytic production of optically active amino acids and their derivatives. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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