Lluis C, Bozal J
Biochim Biophys Acta. 1978 Apr 12;523(2):273-82. doi: 10.1016/0005-2744(78)90031-1.
Chicken liver lactate dehydrogenase L-lactate : NAD+ oxidoreductase, EC1.1.1.27) reversibly catalyses the conversion of hydroxypyruvate to L-glycerate. The variation of the initial reaction rate with the substrate or coenzyme (NADH) concentration together with the inhibition caused by the reaction products and excess substrates, reveal that the kinetic mechanism of the reaction, with hydroxypyruvate as substrate, is of the rapid-equilibrium, ordered-ternary-complex type; NADH is the first substrate in the reaction sequence. Rate equations have been developed for the hydroxypyruvate.E.NADH system without inhibitors, with excess substrates, and with reaction products. Comparison of the rate equations obtained with those calculated theoretically from an ordered-ternary-complex mechanism reveals the existence of E.NAD.NADH,E.NAD-hydroxypyruvate and E.hydroxypyruvate complexes.
鸡肝乳酸脱氢酶（L-乳酸：NAD⁺氧化还原酶，EC1.1.1.27）可逆地催化羟基丙酮酸转化为L-甘油酸。初始反应速率随底物或辅酶（NADH）浓度的变化，以及反应产物和过量底物引起的抑制作用，表明以羟基丙酮酸为底物时反应的动力学机制属于快速平衡、有序三元复合物类型；NADH是反应序列中的第一个底物。已经针对无抑制剂、有过量底物和有反应产物的羟基丙酮酸·E·NADH系统推导了速率方程。将得到的速率方程与从有序三元复合物机制理论计算得到的方程进行比较，揭示了E·NAD·NADH、E·NAD-羟基丙酮酸和E·羟基丙酮酸复合物的存在。
