期刊名称:Journal of Clinical Biochemistry and Nutrition
印刷版ISSN:0912-0009
电子版ISSN:1880-5086
出版年度:1987
卷号:3
期号:1
页码:1-9
DOI:10.3164/jcbn.3.1
出版社:The Society for Free Radical Research Japan
摘要:A glucokinase (EC 2.7.1.2) was purified from Bacillus stearothermophilus , a moderate thermophile. The native glucokinase, M r 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 K m 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 K m values for glucose and ATP, and the lack of ATPase activity make this enzyme advantageous for use in clinical chemical analysis.
关键词:glucokinase;thermophilic bacterium;purification of glucokinase;properties of glucokinase