Ostrovtsova S A, Strumilo S A
Vopr Med Khim. 1991 Jan-Feb;37(1):70-1.
Kinetics of lipoamide dehydrogenase catalyzed reaction is described by Michaelis-Menten equation if concentrations of NAD and dihydrolipoamide (DLA) varied. Effective Km values were equal to 0.11 mM for NAD and 0.50 mM for DLA, respectively. Kinetic indications of positive cooperation between sites binding both NAD and DLA were manifested in presence of NADH. Apparent Ki value for NADH constituted 0.88-0.10 mM, thus demonstrating the effective regulation of the lipoamide dehydrogenase activity by end products.
如果烟酰胺腺嘌呤二核苷酸（NAD）和二氢硫辛酰胺（DLA）的浓度发生变化，硫辛酰胺脱氢酶催化反应的动力学可用米氏方程来描述。对于NAD，有效米氏常数（Km）值分别为0.11 mM，对于DLA则为0.50 mM。在烟酰胺腺嘌呤二核苷酸磷酸（NADH）存在的情况下，结合NAD和DLA的位点之间表现出正协同作用的动力学迹象。NADH的表观抑制常数（Ki）值为0.88 - 0.10 mM，从而证明了终产物对硫辛酰胺脱氢酶活性的有效调节。
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