论米凯利安动力学的普遍性。

On the generality of Michaelian kinetics.

作者信息

Barel Itay, Brown Frank L H

机构信息

Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA and Department of Physics, University of California, Santa Barbara, California 93106, USA.

出版信息

J Chem Phys. 2017 Jan 7;146(1):014101. doi: 10.1063/1.4973220.

DOI:10.1063/1.4973220

PMID:28063450

Abstract

The reversible Michaelis-Menten equation is shown to follow from a very broad class of steady-state kinetic models involving enzymes that adopt a unique free (i.e., not complexed to substrate/product) state in solution. In the case of enzymes with multiple free states/conformations (e.g., fluctuating, hysteretic, or co-operative monomeric enzymes), Michaelian behavior is still assured if the relative steady-state populations of free enzyme states are independent of substrate and product concentration. Prior models for Michaelian behavior in multiple conformer enzymes are shown to be special cases of this single condition.

摘要

可逆的米氏方程被证明可从一类非常广泛的稳态动力学模型推导得出，这类模型涉及在溶液中呈现独特自由（即未与底物/产物结合）状态的酶。对于具有多种自由状态/构象的酶（例如波动的、滞后的或协同的单体酶），如果自由酶状态的相对稳态群体与底物和产物浓度无关，米氏行为仍然可以保证。先前关于多构象酶米氏行为的模型被证明是这种单一条件的特殊情况。