Enzymatic Preparation of an (S)-Amino Acid from a Racemic Amino Acid
| Autor: | Animesh Goswami, Ronald L. Hanson, Ramesh N. Patel, Thomas P. Tully, Yijun Chen, Iqbal Gill, Michael A. Montana, William L. Parker, Steven L. Goldberg |
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| Rok vydání: | 2010 |
| Předmět: |
chemistry.chemical_classification
biology Stereochemistry Organic Chemistry Dehydrogenase Formate dehydrogenase biology.organism_classification Reductive amination Cofactor Amino acid chemistry.chemical_compound Propanoic acid chemistry biology.protein Formate Physical and Theoretical Chemistry Sporosarcina ureae |
| Zdroj: | Organic Process Research & Development. 15:241-248 |
| ISSN: | 1520-586X 1083-6160 |
| Popis: | The (S)-amino acid, (S)-2-amino-3-(6-o-tolylpyridin-3-yl)propanoic acid (3), is a key intermediate needed for synthesis of an antidiabetic drug candidate. Three enzymatic routes to 3 were explored. (S)-Amino acid 3 could be prepared in 73% isolated yield with 99.9% ee from racemic amino acid 1 using (R)-amino acid oxidase from Trigonopsis variabilis expressed in Escherichia coli in combination with an (S)-aminotransferase using (S)-aspartate as amino donor. The (S)-aminotransferase was purified from a soil organism identified as Burkholderia sp. and cloned and expressed in E. coli. (S)-Amino acid 3 with 100% ee was also prepared in 68% solution yield and 54% isolated yield from 1 using recombinant (R)-amino acid oxidase from T. variabilis and an (S)-amino acid dehydrogenase from Sporosarcina ureae. The cofactor NADH required for the reductive amination reaction was regenerated using formate and formate dehydrogenase. The chemoenzymatic dynamic resolution of 1 by (R)-selective oxidation with Celite-immobil... |
| Databáze: | OpenAIRE |
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