吉林大学学报（理学版）2017，Vol.55Issue(6)：1614-1620,7.DOI:10.13413/j.cnki.jdxblxb.2017.06.48
北京棒杆菌天冬氨酸激酶突变体P184Q的酶学性质表征
Characterization of Enzymatic Properties of Mutant P184Q of Aspartate Kinase from Corynebacterium pekinense
摘要
Abstract
By analyzing the structure of aspartate kinase (AK),we screened the Pro184 site that might affect the binding of allosteric inhibitors,and the mutant strain P184Q was successfully screened by saturation site-directed mutagenesis.The enzymatic properties show that the V max of P184Q was 3 times higher than that of wide-type (WT),n=1.39 indicating that the positive cooperativity of the substrate decreased, the K m value decreased simultaneously, and the affinity of the substrate increased.The optimum pH of P184Q was 6.5.The optimum temperature of P184Q was 25 ℃.The half-life period was 2.8 h.Futhermore,P184Q show strong resistance to metal ions,organic solvent and inhibitors Thr+Met,Lys+Met,Thr+Lys and Lys.关键词
北京棒杆菌/天冬氨酸激酶/突变体/酶学性质Key words
Corynebacterium pekinense/aspartate kinase/mutant/enzymatic property分类
生物科学引用本文复制引用
方丽,王锐楠,詹冬玲,张芷睿,闵伟红..北京棒杆菌天冬氨酸激酶突变体P184Q的酶学性质表征[J].吉林大学学报（理学版）,2017,55(6):1614-1620,7.基金项目
国家高技术研究发展计划"863"项目基金(批准号:2013AA20112206-2)和吉林省科技创新人才培育计划项目(批准号:20150519012JH). （批准号:2013AA20112206-2）
