Takamiya S, Fukui T
J Biochem. 1978 Sep;84(3):569-74. doi: 10.1093/oxfordjournals.jbchem.a132161.
The chemical and catalytic properties of potato phosphoglucomutase [EC 2.7.5.1] were studied using various enzyme species (Peaks Ia, Ib, Ic, and II; Takamiya, S. & Fukui, T. (1978) Plant Cell Physiol. 19, 319--328). The molecular weights of the species are all approximately 60,000. No indication of the presence of subunit structure was obtained under various conditions. The amino acid composition of Peak Ia is generally similar to those of the enzymes from other sources, though it has some peculiarities. The Peak Ia and Peak II enzymes both absolutely require alpha-D-glucose 1,6-bisphosphate and Mg2+ for activity, and appear to have a "ping-pong" mechanism. A low concentration of Be2+ inhibits their action, the inhibition being retarded either by Mg2 or EDTA. Although the inhibition patterns by various metabolites, are similar for Peaks Ia and II, they differ in their kinetic parameters and optimal pH values.
利用多种酶种类（峰Ia、峰Ib、峰Ic和峰II；高宫，S.和福井，T.（1978年）《植物细胞生理学》19卷，319 - 328页）研究了马铃薯磷酸葡萄糖变位酶[EC 2.7.5.1]的化学和催化特性。这些酶种类的分子量均约为60,000。在各种条件下均未发现亚基结构存在的迹象。峰Ia的氨基酸组成总体上与其他来源的酶相似，不过有一些独特之处。峰Ia和峰II这两种酶的活性都绝对需要α - D - 葡萄糖1,6 - 二磷酸和Mg2 +，并且似乎具有“乒乓”机制。低浓度的Be2 +会抑制它们的作用，Mg2 +或EDTA可延缓这种抑制作用。尽管峰Ia和峰II对各种代谢物的抑制模式相似，但它们的动力学参数和最适pH值有所不同。
