中文摘要：

MATTt (从 Thermus thermophilus HB27 的 thermostable 蛋氨酸 adenosyltransferase ) 是在 Escherchia coli 的 overexpressed 并且净化了使用 Ni-NTA 亲密关系列。MATTt 的酶的活动从 30 在一个温度范围被调查

英文摘要：

MATTt （a thermostable methionine adenosyl- transferase from Thermus thermophilus HB27） was over- expressed in Escherchia coli and purified using Ni-NTA affinity column. The enzymatic activity of MATTt was investigated in a temperature range from 30 ℃ to 90 ℃, showing that MATTt exhibited a high enzymatic activity and good thermostability at 80 ℃. Circular dichroism spectra reveals that MATTt contains high portion of β- sheet structures contributing to the thermostability of MATTt. The kinetic parameter, Km is 4.19 mmoFL and 1.2 mmol/L for ATP and methionine, respectively. MATTt exhibits the highest enzymatic activity at pH 8. Cobalt （Co^2＋） and zinc ion （Zn^2＋） enhances remarkably the activity of MATTt compared to the magnesium ion （Mg^2＋）. All these results indicated that the thermostable MATTt has great potential for industry applications.