通过定点饱和突变工程化嗜热双歧杆菌中的间二氨基庚二酸脱氢酶用于 D-苯丙氨酸的合成。
Engineering the meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum by site saturation mutagenesis for D-phenylalanine synthesis.
机构信息
National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, China.
出版信息
Appl Environ Microbiol. 2013 Aug;79(16):5078-81. doi: 10.1128/AEM.01049-13. Epub 2013 May 31.
Abstract
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.
摘要
为了扩大嗜热栖热菌中中间二氨基庚二酸脱氢酶的基质结合口袋，以容纳更大的 2-酮酸，针对四个氨基酸残基（F146、T171、R181 和 H227）进行了定点饱和突变。在所有突变体中，单突变体 H227V 的比活为 2.39 ± 0.06 U·mg(-1)，比野生型酶提高了 35.1 倍。
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