β-Aryl-β-amino acid aminotransferase from Variovorax sp. JH2 is useful for enantioselective β-phenylalanine production
| Autor: | Jun Shima, Makoto Hibi, Jun Ogawa, Junichi Mano, Sakayu Shimizu, Tairo Hagishita |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
chemistry.chemical_classification
biology Transamination Stereochemistry Stereoselective synthesis Bioengineering Phenylalanine Fast protein liquid chromatography Variovorax biology.organism_classification Applied Microbiology and Biotechnology Amino acid Enzyme Biochemistry chemistry biology.protein Propionate β-Phenylalanine aminotransferase Citrate synthase β-Aryl-β-amino acid aminotransferase Variovorax sp Agronomy and Crop Science Food Science Biotechnology |
| Zdroj: | Biocatalysis and Agricultural Biotechnology. 1(3):253-258 |
| ISSN: | 1878-8181 |
| Popis: | A bacterium, Variovorax sp. JH2, has an ability to degrade (S)-β-phenylalanine stereoselectively. The enzyme involved in the degradation, (S)-β-phenylalanine:2-oxoglutarate aminotransferase, was purified to homogeneity from Variovorax sp. JH2 and characterized. The enzyme was useful for (R)-β-phenylalanine production from racemic β-phenylalanine by enantioselective decomposition of (S)-β-phenylalanine through transamination. (S)-β-Phenylalanine and (S)-3-amino-3-(3-pyridyl)propionate served as good amino-donors in the transamination and 2-oxoglutarate, oxaloacetate, pyruvate, and 1,3-acetonedicarboxylate served as amino-acceptors. The enzyme had a molecular weight of about 72,000 and consisted of two identical subunits. Three internal amino acid sequences (54, 67, and 63 residues) were determined and showed homology with glutamate-1-semialdehyde 2,1-aminomutases. |
| Databáze: | OpenAIRE |
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