Yoshida I, Koyama T, Ogura K
Chemical Research Institute of Non-Aqeous Solutions, Tohoku University, Sendai, Japan.
Biochem Biophys Res Commun. 1989 Apr 28;160(2):448-52. doi: 10.1016/0006-291x(89)92453-4.
Formation of a stable complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26, which represents the catalytically active state of this enzyme, is observed in the presence of a relatively high concentrations of inorganic pyrophosphate or one of the substrates, isopentenyl diphosphate or farnesyl diphosphate. The apparent molecular mass of the complex is estimated to be about 50 kDa by gel filtration with Superose 12.
在存在相对高浓度的无机焦磷酸或底物之一（异戊烯基二磷酸或法呢基二磷酸）的情况下，观察到来自藤黄微球菌B-P 26的十六异戊二烯基二磷酸合酶的两个必需组分形成了稳定的复合物，该复合物代表了这种酶的催化活性状态。通过使用Superose 12进行凝胶过滤，估计该复合物的表观分子量约为50 kDa。
