高等植物叶片中的L-乳酸脱氢酶。生菜（Lactuca sativa L.）中该酶的动力学与调控
L-Lactate dehydrogenase from leaves of higher plants. Kinetics and regulation of the enzyme from lettuce (Lactuca sativa L).
作者信息
Betsche T
出版信息
Biochem J. 1981 Jun 1;195(3):615-22. doi: 10.1042/bj1950615.
Abstract
- L-Lactate dehydrogenase from lettuce (Lactuca sativa) leaves was purified to electrophoretic homogeneity by affinity chromatography. 2. In addition to its NAD(H)-dependent activity with L-lactate and pyruvate, the enzyme also catalyses the reduction of hydroxypyruvate and glyoxylate. The latter activities are not due to a contamination of the enzyme preparations with hydroxypyruvate reductase. 3. The enzyme shows allosteric properties that are markedly by the pH. 4. ATP is a potent inhibitor of the enzyme. The kinetic data suggest that the inhibition by ATP is competitive with respect to NADH at pH 7.0 and 6.2. The existence of regulatory binding sites for ATP and NADH is discussed. 5. Bivalent metal cations and fructose 6-phosphate relieve the ATP inhibition of the enzyme. 6. A function of leaf L-lactate dehydrogenase is proposed as a component of the systems regulating the cellular pH and/or controlling the concentration of reducing equivalents in the cytoplasm of leaf cells.
摘要
- 通过亲和色谱法将来自生菜（莴苣）叶片的L-乳酸脱氢酶纯化至电泳纯。2. 除了对L-乳酸和丙酮酸具有依赖NAD(H)的活性外，该酶还催化羟基丙酮酸和乙醛酸的还原。后一种活性并非由于酶制剂被羟基丙酮酸还原酶污染所致。3. 该酶表现出受pH显著影响的别构性质。4. ATP是该酶的有效抑制剂。动力学数据表明，在pH 7.0和6.2时，ATP的抑制作用相对于NADH是竞争性的。文中讨论了ATP和NADH的调节性结合位点的存在。5. 二价金属阳离子和6-磷酸果糖可解除ATP对该酶的抑制。6. 提出叶片L-乳酸脱氢酶的一个功能是作为调节细胞pH和/或控制叶片细胞细胞质中还原当量浓度的系统的一个组成部分。
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