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A thermoresistant gluconokinase encoded by the gntK gene of Escherichia coli K-12 was purified and characterized. The K m values of the purified enzyme for gluconate and ATP are 42 μM and 123 μM, respectively, and the activity was not altered by the presence of pyruvate. The enzyme was shown to function as a dimer with two identical subunits of 18.4 kDa. These characteristics appear to...
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