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National Chung Hsing University Institutional Repository - NCHUIR > 生命科學院 > 生物化學研究所 > 依資料類型分類 > 期刊論文 >  Asymmetrical synthesis of L-homophenylalanine using engineered Escherichia coli aspartate aminotransferase

Please use this identifier to cite or link to this item: http://nchuir.lib.nchu.edu.tw/handle/309270000/130813

標題: Asymmetrical synthesis of L-homophenylalanine using engineered Escherichia coli aspartate aminotransferase
作者: Lo, H.H.;Hsu, S.K.;Lin, W.D.;Chan, N.L.;Hsu, W.H.
詹迺立
關鍵字: site-directed mutagenesis;substrate-specificity;kinetic resolution;amino-acids;biosynthesis;esters
日期: 2005
Issue Date: 2012-12-07 16:08:24 (UTC+8)
關連: Biotechnology Progress, Volume 21, Issue 2, Page(s) 411-415.
摘要: Site-directed mutagenesis was performed to change the substrate specificity of Escherichia coli aspartate aminotransferase (AAT). A double mutant, R292E/L18H, with a 12.9-fold increase in the specific activity toward L-lysine and 2-oxo-4-phenylbutanoic acid (OPBA) was identified. E. coli cells expressing this mutant enzyme could convert OPBA to L-homophenylalanine (L-HPA) with 97% yield and more than 99.9% ee using L-lysine as amino donor. The transamination product Of L-lysine, 2-keto-6-aminocaproate, was cyclized nonenzymatically to form Delta(1)-piperideine 2-carboxylic acid in the reaction mixture. The low solubility of L-HPA and spontaneous cyclization of 2-keto-6-aminocaproate drove the reaction completely toward L-HPA production. This is the first aminotransferase process using L-lysine as inexpensive amino donor for the L-HPA production to be reported.
Relation: Biotechnology Progress
Appears in Collections:[依資料類型分類] 期刊論文
[依教師分類] 詹迺立

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