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|標題:||Asymmetrically Simultaneous Synthesis of L-Homophenylalanine and N-6-Protected-2-oxo-6-amino-hexanoic Acid by Engineered Escherichia coli Aspartate Aminotransferase|
|期刊/報告no：:||Biotechnology Progress, Volume 25, Issue 6, Page(s) 1637-1642.|
|摘要:||L-Homophenylalanine (L-HPA) and N-6-protected-2-oxo-6-amino-hexanoic acid (N-6-protected-OAHA) an be used as building blocks for the manufacture of angiotensin-converting enzyme inhibitors. To synthesize L-HPA and N-6-protected-OAHA simultaneously from 2-oxo-4-phenylbutanoic acid (OPBA) and N-6-protected-L-lysine, several variants of Escherichia coli aspartate aminotransferase (AAT) were developed by site-directed mutagenesis and their catalytic activities were investigated. Three kinds of N-6-protected-L-lysine were tested as potential amino donors for the bioconversion process. AAT variants of R292E/L18H and R292E/L18T exhibited specific activities of 0.70 +/- 0.01 U/mg protein and 0.67 +/- 0.02 U/mg protein to 2-amino-6-tert-butoxycarbonylamino-hexanoic acid (BOC-lysine) and 2-amino-6-(2,2,2-trifluoro-acetylamino)-hexanoic acid, respectively. E. coli cells expressing R292E/L18H variant were able to convert OPBA and BOC-lysine 10 L-HPA and 2-oxo-6-tert-butoxycarbonylamino-hexanoic acid (BOC-OAHA) with 96.2% yield in 8 h. This is the first report demonstrating a process for the simultaneous production of two useful building blocks, L-HPA and BOC-OAHA. (C) 2009 American Institute of Chemical Engineers Biotechnol. Prog., 25: 1637-1642, 2009|
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