A MOFRL family glycerate kinase from the thermophilic crenarchaeon, <Emphasis Type="Italic">Sulfolobus tokodaii</Emphasis>, with unique enzymatic properties |
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| Authors: | Bo Liu Lei Wu Tianming Liu Ye Hong Yulong Shen Jinfeng Ni |
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| Institution: | (1) College of Food and Bioengineering, Shandong Institute of Light Industry, Jinan, 250353, People’s Republic of China;(2) State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, People’s Republic of China; |
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| Abstract: | A glycerate kinase gene (ST2037) from the hyperthermophilic crenarchaeon Sulfolobus tokodaii was cloned and expressed in Escherichia coli. The purified homodimeric protein (45 kDa) specifically catalyzed the formation of 2-phosphoglycerate with d-glycerate as substrate. The thermostable enzyme displayed maximum activity (over 20 min) at 90°C and pH 4.5. The maximal
activity was in the presence of Co2+. The MOFRL family glycerate kinase used AMP as phosphate donor with maximal activity towards GTP. These characteristics of
the enzyme suggested its potential in the catalytic production of 2-phosphoglycerate. |
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