Guarriero-Bobyleva V, Masini A, Volpi-Becchi M A, Cennamo C
Ital J Biochem. 1978 Sep-Oct;27(5):287-99.
The kinetic properties of the cytoplasmic and mitochondrial aconitate hydratases of rat liver have been studied by measuring the formation of the two products from each of the three tricarboxylic acids used as substrate. The kinetic properties of the two enzymes are very similar; the similarity of the Km values for each of the three substrates is particularly remarkable. The results are discussed with particular reference to a possible role of the cytoplasmic aconitate hydratase in the process of gluconeogenesis. With both aconitate hydratases, substrate activation by citrate and D-isocitrate has been observed.
通过测量以三种三羧酸中的每一种作为底物时两种产物的形成情况，研究了大鼠肝脏细胞质和线粒体乌头酸水合酶的动力学特性。这两种酶的动力学特性非常相似；三种底物各自的米氏常数（Km值）的相似性尤为显著。特别参照细胞质乌头酸水合酶在糖异生过程中可能发挥的作用对结果进行了讨论。对于两种乌头酸水合酶，均观察到了柠檬酸和D-异柠檬酸对底物的激活作用。
