The original Michaelis constant: translation of the 1913 Michaelis-Menten paper.
The original Michaelis constant: translation of the 1913 Michaelis-Menten paper.
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DOI：
10.1021/bi201284u
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发表时间：
2011-10-04
期刊：
影响因子：
2.9
通讯作者：
Goody RS
中科院分区：
文献类型：
--
作者：
Michaelis L;Menten ML;Johnson KA;Goody RS
将近100年前，Michaelis和Menten发表了他们现在的经典论文（Michaelis， L., and Menten， M. L. (1913) Die Kinetik der Invertinwirkung, Biochemische Zeitschrift 49, 333-369），他们在论文中表明，酶催化反应的速率与Michaelis-Menten方程预测的酶-底物复合物的浓度成正比。由于原文是用德语写的，但经常被讲英语的作者引用，我们对1913年的出版物进行了完整的翻译，我们将其作为在线补充（http://pubs.acs.org）提供。在这里，我们介绍翻译，描述工作的历史背景，并展示对原始数据的新分析。在这样做的过程中，我们发现了几个惊喜，揭示了酶学早期历史的有趣一瞥。特别是，我们使用现代计算方法对Michaelis和Menten的数据进行了重新分析，揭示了原始出版物中意想不到的严谨性和精确性，并发现了自他们的工作发表以来一个世纪以来被忽视的复杂、全面的分析。Michaelis和Menten不仅分析了初始速度测量值，而且还将他们的全程过程数据拟合到速率方程的积分形式中，包括产物抑制，并推导出一个单一的全局常数来表示他们的所有数据。该常数不是Michaelis常数，而是Vmax/Km，特异性常数乘以酶浓度（kcat/Km*E0）。
Nearly 100 years ago Michaelis and Menten published their now classic paper (Michaelis, L., and Menten, M. L. (1913) Die Kinetik der Invertinwirkung, Biochemische Zeitschrift 49, 333–369), in which they show that the rate of an enzyme-catalyzed reaction is proportional to the concentration of enzyme-substrate complex predicted by the Michaelis-Menten equation. Because the original text was written in German, yet is often quoted by English speaking authors, we undertook a complete translation of the 1913 publication, which we provide as an online supplement (http://pubs.acs.org). Here we introduce the translation, describe the historical context of the work, and show a new analysis of the original data. In doing so, we uncovered several surprises that reveal an interesting glimpse into the early history of enzymology. In particular, our re-analysis of Michaelis and Menten’s data using modern computational methods revealed an unanticipated rigor and precision in the original publication and uncovered a sophisticated, comprehensive analysis that has been overlooked in the century since their work was published. Michaelis and Menten not only analyzed initial velocity measurements, but they also fit their full time course data to the integrated form of the rate equations, including product inhibition, and derived a single global constant to represent all of their data. That constant was not the Michaelis constant, but rather, Vmax/Km, the specificity constant times the enzyme concentration (kcat/Km*E0).
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