Báo cáo khoa học: A novel hyperthermostable 5¢-deoxy-5¢-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus
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We report herein the first molecular characterization of 5¢-deoxy-5¢-methyl-thio-adenosine phosphorylase II from Sulfolobus solfataricus(SsMTAPII). The isolated gene of SsMTAPII was overexpressed inEscherichia coli BL21. Purified recombinant SsMTAPII is a homohexamer of 180 kDa with an extremely low Km(0.7lm) for 5¢-deoxy-5¢-methylthioadenosine. The enzyme is highly thermophilic with an optimum temperature of 120C and extremely thermostable with an apparent Tmof 112C that increases in the presence of substrates....
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