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The reaction catalysed by an enzyme uses exactly the same reactants and produces exactly the same products as the uncatalysed reaction. Like other catalysts, enzymes do not alter the position of equilibrium between substrates and products. [1] However, unlike uncatalysed chemical reactions, enzyme-catalysed reactions display saturation kinetics.
The plot is occasionally attributed to Augustinsson [5] and referred to the Woolf–Augustinsson–Hofstee plot [6] [7] [8] or simply the Augustinsson plot. [9] However, although Haldane, Woolf or Eadie were not explicitly cited when Augustinsson introduced the versus / equation, both the work of Haldane [10] and of Eadie [3] are cited at other places of his work and are listed in his ...
An illustration to show (a) Alberty-Hammes-Eigen model, and (b) Chou's model, where E denotes the enzyme whose active site is colored in red, while the substrate S in blue. The theory of diffusion-controlled reaction was originally utilized by R.A. Alberty, Gordon Hammes, and Manfred Eigen to estimate the upper limit of enzyme-substrate reaction.
In biochemistry, a rate-limiting step is a reaction step that controls the rate of a series of biochemical reactions. [1] [2] The statement is, however, a misunderstanding of how a sequence of enzyme-catalyzed reaction steps operate. Rather than a single step controlling the rate, it has been discovered that multiple steps control the rate.
In biochemistry, a Hanes–Woolf plot, Hanes plot, or plot of / against is a graphical representation of enzyme kinetics in which the ratio of the initial substrate concentration to the reaction velocity is plotted against .
Diffusion-controlled (or diffusion-limited) reactions are reactions in which the reaction rate is equal to the rate of transport of the reactants through the reaction medium (usually a solution). [1] The process of chemical reaction can be considered as involving the diffusion of reactants until they encounter each other in the right ...
Regulatory enzymes are commonly the first enzyme in a multienzyme system: the product of the reaction catalyzed by the first enzyme is the substrate of the second enzyme, so the cell can control the amount of resulting product by regulating the activity of the first enzyme of the pathway.
The amount of substrate needed to achieve a given rate of reaction is also important. This is given by the Michaelis–Menten constant (K m), which is the substrate concentration required for an enzyme to reach one-half its maximum reaction rate; generally, each enzyme has a characteristic K M for a given substrate.