کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2075541 | 1079340 | 2012 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: β-Aryl-β-amino acid aminotransferase from Variovorax sp. JH2 is useful for enantioselective β-phenylalanine production β-Aryl-β-amino acid aminotransferase from Variovorax sp. JH2 is useful for enantioselective β-phenylalanine production](/preview/png/2075541.png)
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.
Journal: Biocatalysis and Agricultural Biotechnology - Volume 1, Issue 3, July 2012, Pages 253–258