Hill C M, Waight R D, Bardsley W G
Mol Cell Biochem. 1977 May 3;15(3):173-8. doi: 10.1007/BF01734107.
A literature search has been conducted to see to what extent steady-state kinetics studies in the period 1965-1976 have revealed deviations from Michaelis-Menten kinetics. It was found that over 800 enzymes have been reported as giving complex curves for a variety of reasons and a group by group classification of all these enzymes has been carried out listing all the types of variations reported and the authors' explanations. In addition, for highly complex curves, we have determined the minimum degree of the rate equation. There were very few determined attempts to demonstrate adherence to the Michaelis-Menten equation over a wide variety of experimental conditions and substrate concentration and almost invariably detailed experimental work revealed unsuspected complexities. For these reasons, it is concluded that the assumption that most enzymes follow the Michaelis-Menten equation can not be supported by an appeal to the literature.
已进行文献检索，以了解1965年至1976年期间的稳态动力学研究在多大程度上揭示了与米氏动力学的偏差。结果发现，有超过800种酶因各种原因被报道给出复杂曲线，并且已对所有这些酶进行了逐组分类，列出了所报道的各种变异类型以及作者的解释。此外，对于高度复杂的曲线，我们已经确定了速率方程的最低次数。几乎没有确定的尝试在各种实验条件和底物浓度下证明符合米氏方程，而且几乎总是详细的实验工作揭示出意想不到的复杂性。基于这些原因，可以得出结论，即大多数酶遵循米氏方程这一假设无法从文献中得到支持。
