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乳酸脱氢酶与其底物反应某些步骤的解析。

The resolution of some steps of the reactions of lactate dehydrogenase with its substrates.

作者信息

Heck H D, McMurray C H, Gutfreund H

出版信息

Biochem J. 1968 Aug;108(5):793-6. doi: 10.1042/bj1080793.

Abstract
  1. The reaction of pig heart lactate dehydrogenase (EC 1.1.1.27) with NAD(+) and lactate to form pyruvate and NADH was followed by rapid spectrophotometric methods. The distinct spectrum of enzyme-bound NADH permits the measurement of the rate of dissociation of this compound. 2. The reduction of the first mole equivalent of NAD(+) per mole of enzyme sites can also be observed, and is much more rapid than the steady-state rate of NADH production. 3. At pH8 the dissociation of the enzyme-NADH complex is rate-determining for the steady-state oxidation of lactate. At lower pH some other step after the interconversion of the ternary complex and before the dissociation of NADH is rate-determining. Other evidence for a compulsory-order mechanism is provided.
摘要
  1. 采用快速分光光度法跟踪猪心乳酸脱氢酶(EC 1.1.1.27)与NAD⁺和乳酸反应生成丙酮酸和NADH的过程。酶结合的NADH独特的光谱使得能够测量该化合物的解离速率。2. 还可以观察到每摩尔酶位点上第一摩尔当量的NAD⁺的还原,其比NADH产生的稳态速率快得多。3. 在pH8时,酶 - NADH复合物的解离是乳酸稳态氧化的速率决定步骤。在较低pH值下,三元复合物相互转化后且NADH解离之前的其他步骤是速率决定步骤。还提供了强制顺序机制的其他证据。

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[Structural flexibility and enzyme function].
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Structural adaptations of lactate dehydrogenase isozymes.乳酸脱氢酶同工酶的结构适应性
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