%A Yanhui Liu,Biqiang Chen,Zheng Wang,Luo Liu,Tianwei Tan %T Functional characterization of a thermostable methionine adenosyltransferase from Thermus thermophilus HB27 %0 Journal Article %D 2016 %J Front. Chem. Sci. Eng. %J Frontiers of Chemical Science and Engineering %@ 2095-0179 %R 10.1007/s11705-016-1566-2 %P 238-244 %V 10 %N 2 %U {https://journal.hep.com.cn/fcse/EN/10.1007/s11705-016-1566-2 %8 2016-05-19 %X

MATTt (a thermostable methionine adenosyltransferase from Thermus thermophilus HB27) was overexpressed in Escherchia coli and purified using Ni-NTA affinity column. The enzymatic activity of MATTt was investigated in a temperature range from 30 °C to 90 °C, showing that MATTt exhibited a high enzymatic activity and good thermostability at 80 °C. 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 mmol/L and 1.2 mmol/L for ATP and methionine, respectively. MATTt exhibits the highest enzymatic activity at pH 8. Cobalt (Co2+) and zinc ion (Zn2+) enhances remarkably the activity of MATTt compared to the magnesium ion (Mg2+). All these results indicated that the thermostable MATTt has great potential for industry applications.