Korte I, Hockwin O, Ohrloff C, Schmidt G, Fuss R
Arzneimittelforschung. 1977;27(8):1532-4.
The Michaelis-Menten constant for fumarase (E.C. 4.2.1.2) has been determined by measuring the enzyme activity by the spectrophotometric method of Racker, which depends on the formation or disappearance of the double bond of fumaric acid. When using Na2-fumarate or bencyclan hydrogenfumarate (Fludilat), respectively, as a substrate, a KM-value of 1.3 X 10(-3) M was found for both substances. In a linked assay where the formation of NADH in the reaction of fumarate leads to malate leads to oxaloacetate was used as a parameter for the reaction rate, a KM-value of 1.35 X 10(-3) M was found.
延胡索酸酶(E.C. 4.2.1.2)的米氏常数已通过Racker的分光光度法测量酶活性来确定,该方法取决于富马酸双键的形成或消失。当分别使用富马酸钠或苄环烷氢富马酸盐(氟桂利嗪)作为底物时,两种物质的KM值均为1.3×10⁻³ M。在一个连锁测定中,以富马酸盐反应生成苹果酸再生成草酰乙酸过程中NADH的形成作为反应速率的参数,发现KM值为1.35×10⁻³ M。