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盐对D-甘油酸脱氢酶动力学行为的影响。

Effect of salts on D-glycerate dehydrogenase kinetic behavior.

作者信息

Coderch R, Lluis C, Bozal J

出版信息

Biochim Biophys Acta. 1979 Jan 12;566(1):21-31. doi: 10.1016/0005-2744(79)90244-4.

DOI:10.1016/0005-2744(79)90244-4
PMID:31939
Abstract

Bovine liver D-glycerate dehydrogenase (D-glycerate:NAD (NADP) oxidoreductase, EC 1.1.1.29) adapts its kinetic behaviour to a sequential mechanism. The presence of NaCl causes an appreciable variation in the Km and V values. relative to the both substrates in the hydroxypyruvate/D-glycerate dehydrogenase/NADH system, which does not happen in the D-glycerate/D-glycerate dehydrogenase/NAD system. The former system is inhibited by high concentrations of NaCl and activated by low salt concentrations. The hydroxypyruvate concentration causing substrate inhibition increases as the concentration of NaCl increases; excess NADH inhibition is independent of the salt concentration. The variation of the initial rates of both systems, in the presence of chlorides having monovalent and divalent cations, or sodium halides, Na2SO4 and NaNO3 (at constant ionic strength) suggests that the anions have a specific action on the enzyme. An increase in the NaCl concentration causes a displacement of the optimum D-glycerate dehydrogenase pH (with hydroxypyruvate and NADH as substrates) towards the acid area. The enzyme stability, at varying pH, varies with the salt concentration.

摘要

牛肝D-甘油酸脱氢酶(D-甘油酸:NAD(NADP)氧化还原酶,EC 1.1.1.29)使其动力学行为适应顺序机制。NaCl的存在会导致Km和V值发生明显变化。相对于羟基丙酮酸/D-甘油酸脱氢酶/NADH系统中的两种底物而言,在D-甘油酸/D-甘油酸脱氢酶/NAD系统中则不会出现这种情况。前一个系统受到高浓度NaCl的抑制,并被低盐浓度激活。导致底物抑制的羟基丙酮酸浓度会随着NaCl浓度的增加而升高;过量NADH抑制与盐浓度无关。在存在单价和二价阳离子的氯化物或卤化钠、Na2SO4和NaNO3(在恒定离子强度下)时,两个系统的初始速率变化表明阴离子对该酶具有特定作用。NaCl浓度的增加会使最佳D-甘油酸脱氢酶pH值(以羟基丙酮酸和NADH为底物)向酸性区域移动。在不同pH值下,酶的稳定性会随盐浓度而变化。

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