Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/68275
標題: Asymmetrically Simultaneous Synthesis of L-Homophenylalanine and N-6-Protected-2-oxo-6-amino-hexanoic Acid by Engineered Escherichia coli Aspartate Aminotransferase
作者: Lo, H.H.
Lin, W.D.
Hsu, S.K.
Hsu, W.H.
關鍵字: aspartate aminotransferase
L-homophenylanine
bioconversion
2-oxo-6-tertbutoxycarbonylamino-hexanonic acid
l-lysine
substrate-specificity
amino-acids
enzyme
oxidase
site
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
URI: http://hdl.handle.net/11455/68275
ISSN: 8756-7938
文章連結: http://dx.doi.org/10.1002/btpr.272
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