Okuda J, Miwa I, Inagaki K
Enzyme. 1984;31(3):176-80. doi: 10.1159/000469520.
The D-glucose anomeric preference of hexokinases partially purified from animals (rat, mouse, and chicken) and baker's yeast (Saccharomyces cerevisiae) were investigated by the assay system with glucose-6-phosphate dehydrogenase as a coupling enzyme. With low Km hexokinases in animal tissues and cells, the ratios of Vmax for the beta-anomer to Vmax for the alpha-anomer (V beta/V alpha) were within a range from 1.3 to 1.5. In yeast, the V beta/V alpha value was 1.1 for hexokinase A, 0.8 for hexokinase B, and 1.4 for glucokinase. The possible explanation for D-glucose anomeric preference of hexokinase is discussed.
利用以葡萄糖-6-磷酸脱氢酶作为偶联酶的检测系统，研究了从动物（大鼠、小鼠和鸡）和面包酵母（酿酒酵母）中部分纯化得到的己糖激酶对D-葡萄糖异头物的偏好性。对于动物组织和细胞中的低Km己糖激酶，β-异头物的Vmax与α-异头物的Vmax之比（Vβ/Vα）在1.3至1.5的范围内。在酵母中，己糖激酶A的Vβ/Vα值为1.1，己糖激酶B的为0.8，葡萄糖激酶的为1.4。文中讨论了己糖激酶对D-葡萄糖异头物偏好性的可能解释。
