Cloning, purification, and characterization of thermostable hypoxanthine-guanine phosphoribosyltransferase from Thermoanaerobacter tengcongensis |
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| Authors: | Chen Qiang You Delin Hu Meihao Gu Xiaocheng Luo Ming Lu Shanyun |
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| Institution: | Laboratory of Structural Biology, College of Life Sciences, Peking University, Beijing 100871, PR China. |
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| Abstract: | Hypoxanthine-guanine phosphoribosyltransferase (HGPRT, EC 2.4.2.8) from a newly characterized thermophile Thermoanaerobacter tengcongensis was expressed in Escherichia coli and purified. Analytical gel filtration suggested that the enzyme exist as a homotetramer in solution. The optimal pH for the forward reaction was found to be 8.0 and the optimal temperature 70 degrees C. The steady-state kinetic characteristics suggest that hypoxanthine is the most effective substrate. This enzyme showed a half-life of 75min at 50 degrees C and no apparent loss of activity after 3 months at 4 degrees C. |
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| Keywords: | Hypoxanthine– guanine phosphoribosyltransferase Thermoanaerobacter tengcongensis Enzyme kinetics Thermostable |
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