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Abstract. The ATP-dependent 6-phosphofructokinase (ATP-PFK) of the hyperthermophilic bacterium Thermotoga maritima was purified 730-fold to homogeneity. The enzyme is a 140-kDa homotetramer composed of 34kDa subunits. Kinetic constants were determined for all substrates in both reaction directions at pH7 and at 75C. Rate dependence (forward reaction) on fructose 6-phosphate (F-6-P) showed sigmoidal...
Abstract. The gene (ORF APF0012) encoding the ATP-dependent 6-phosphofructokinase (ATP-PFK) of the hyperthermophilic archaeon Aeropyrum pernix was identified, cloned, and functionally expressed in Escherichia coli. The deduced amino acid sequence showed similarity (2540%) to members of PFK-B sugar kinases. The purified recombinant enzyme is a heterotetramer of 115kDa, composed of 34-kDa subunits....
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