Maitra P K, Lobo Z
Mol Cell Biochem. 1977 Nov 25;18(1):21-7. doi: 10.1007/BF00215275.
Glucokinase from baker's yeast has been purified to homogeneity. The molecular weight of the subunit is 51,000. The native enzyme sediments with S20,w values in the range of 19 to nearly 4S. The presence of glucose and phosphate favors the heavier species while ATP causes depolymerization. Titration experiments with the Ellman reagent support this view. The enzyme subunit has four sulfhydryl residues of which one is more reactive than the other three. However, it does not seem to be directly responsible for the catalytic activity. The amino acid composition of the enzyme is similar to those of the hexokinases P1 and P2 but for aspartic acid and histidine.
面包酵母中的葡萄糖激酶已被纯化至同质。亚基的分子量为51,000。天然酶的沉降系数S20,w值在19至近4S范围内。葡萄糖和磷酸盐的存在有利于较重的物种，而ATP会导致解聚。用埃尔曼试剂进行的滴定实验支持这一观点。酶亚基有四个巯基残基，其中一个比其他三个更具反应性。然而，它似乎并不直接负责催化活性。该酶的氨基酸组成与己糖激酶P1和P2相似，但天冬氨酸和组氨酸除外。
