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The study of enzyme kinetics is important for two basic reasons. Firstly, it helps explain how enzymes work, and secondly, it helps predict how enzymes behave in living organisms. The kinetic constants defined above, K M and V max, are critical to attempts to understand how enzymes work together to control metabolism.
A decade before Michaelis and Menten, Victor Henri found that enzyme reactions could be explained by assuming a binding interaction between the enzyme and the substrate. [11] His work was taken up by Michaelis and Menten, who investigated the kinetics of invertase, an enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose. [12]
Reversible Michaelis–Menten kinetics, using the reversible form of the Michaelis–Menten equation, is therefore important when developing computer models of cellular processes involving enzymes. In enzyme kinetics, the Michaelis–Menten kinetics kinetic rate law that describes the conversion of one substrate to one product, is often ...
Enzyme kinetics is the investigation of how enzymes bind substrates and turn them into products. [67] The rate data used in kinetic analyses are commonly obtained from enzyme assays. In 1913 Leonor Michaelis and Maud Leonora Menten proposed a quantitative theory of enzyme kinetics, which is referred to as Michaelis–Menten kinetics. [68]
Human enzymes start to denature quickly at temperatures above 40 °C. Enzymes from thermophilic archaea found in the hot springs are stable up to 100 °C. [13] However, the idea of an "optimum" rate of an enzyme reaction is misleading, as the rate observed at any temperature is the product of two rates, the reaction rate and the denaturation rate.
Eadie–Hofstee plot of v against v/a for Michaelis–Menten kinetics. In biochemistry, an Eadie–Hofstee plot (or Eadie–Hofstee diagram) is a graphical representation of the Michaelis–Menten equation in enzyme kinetics. It has been known by various different names, including Eadie plot, Hofstee plot and Augustinsson plot.
While the Lineweaver–Burk plot has historically been used for evaluation of the parameters, together with the alternative linear forms of the Michaelis–Menten equation such as the Hanes–Woolf plot or Eadie–Hofstee plot, all linearized forms of the Michaelis–Menten equation should be avoided to calculate the kinetic parameters ...
A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.e., substrate specificity). The higher the specificity constant, the more the enzyme "prefers" that substrate. [1] The following equation, known as the Michaelis–Menten model, is used to describe the kinetics of enzymes: