Abstract
The gene (open reading frame (ORF) Tm1469, glk) encoding ATP-dependent ROK ( repressors, ORFs, sugar kinases) glucokinase (ATP-GLK, EC 2.7.1.2) of the hyperthermophilic bacterium Thermotoga maritima was cloned and functionally expressed in Escherichia coli. The purified recombinant enzyme is a homodimer with an apparent molecular mass of 80 kDa composed of 36-kDa subunits. Rate dependence (at 80°C) on glucose and ATP followed Michaelis–Menten kinetics with apparent K m values of 1.0 and 0.36 mM, respectively; apparent V max values were about 370 U mg −1. The enzyme was highly specific for glucose as phosphoryl acceptor. Besides glucose only 2-deoxyglucose was phosphorylated to some extent, whereas mannose and fructose were not used. With a temperature optimum of 93°C the enzyme is the most thermoactive bacterial ATP-GLK described.
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