Journal of Jilin University Science Edition
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FANG Li, WANG Ruinan, ZHAN Dongling, ZHANG Zhirui, MIN Weihong
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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 sitedirected mutagenesis. The enzymatic properties show that the Vmax of P184Q was 3 times higher than that of widetype (WT), n=1.39 indicating that the positive cooperativity of the substrate decreased, the Km 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 halflife 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.
Key words: aspartate kinase, mutant, Corynebacterium pekinense, enzymatic property
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FANG Li, WANG Ruinan, ZHAN Dongling, ZHANG Zhirui, MIN Weihong. Characterization of Enzymatic Properties of Mutant P184Qof Aspartate Kinase from Corynebacterium pekinense[J].Journal of Jilin University Science Edition, 2017, 55(06): 1614-1620.
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http://xuebao.jlu.edu.cn/lxb/EN/Y2017/V55/I06/1614
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