Engineering the meso-Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum by Site Saturation Mutagenesis for D-Phenylalanine Synthesis

摘要：

In order to enlarge the substrate binding pocket of the meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum to accommodate larger 2-keto acids, four amino acid residues (Phe146, Thr171, Arg181, and His227) were targeted for site saturation mutagenesis.Among all mutants, the single mutant H227V had a specific activity of 2.39 ± 0.06 U· mg-1, which was 35.1-fold enhancement over the wild-type enzyme.

作者: Xiuzhen Gao Fang Huang Jinhui Feng Xi Chen Hailing Zhang Zhixiang Wang Qiaqing Wu Dunming Zhu

作者单位: National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalyt College of Chemistry and Chemical Engineering, University of Chinese Academy Sciences, Beijing, Chin National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalyt

会议类型: 国内会议

会议名称: 第七届国际分子模拟与信息技术应用学术会议

会议地点: 苏州

会议语种:英文

页码: 157-160

在线出版日期: 2014-10-26（万方平台首次上网日期，不代表论文的发表时间）