Abstract
A glucokinase (EC 2.7.1.2) was purified from Bacillus stearothermophilus, a moderate thermophile. The native glucokinase, Mr about 68, 000, consists of two identical subunits. This enzyme is relatively temperature- and pH-stable, the optimal pH range for the enzymatic activity being within the stable pH range. It selectively catalyzes the phosphorylation of glucose rather than other kinds of hexoses. The Km values were estimated to be 1×10-4M for glucose and 0.5×10-4M for ATP. It shows no ATPase activity. The high stability, high substrate specificity, low Km values for glucose and ATP, and the lack of ATPase activity make this enzyme advantageous for use in clinical chemical analysis.
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