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In biochemistry, an enzyme substrate is the material upon which an enzyme acts. When referring to Le Chatelier's principle , the substrate is the reagent whose concentration is changed. Spontaneous reaction
Determining the parameters of the Michaelis–Menten equation typically involves running a series of enzyme assays at varying substrate concentrations , and measuring the initial reaction rates , i.e. the reaction rates are measured after a time period short enough for it to be assumed that the enzyme-substrate complex has formed, but that the ...
The substrate concentration midway between these two limiting cases is denoted by K M. Thus, K M is the substrate concentration at which the reaction velocity is half of the maximum velocity. [2] The two important properties of enzyme kinetics are how easily the enzyme can be saturated with a substrate, and the maximum rate it can achieve.
The rate of a reaction is the concentration of substrate disappearing (or product produced) per unit time (mol L −1 s −1). The % purity is 100% × (specific activity of enzyme sample / specific activity of pure enzyme). The impure sample has lower specific activity because some of the mass is not actually enzyme.
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.
where [A] is the fixed concentration of agonist and EC 50 is the concentration of agonist that results in half maximal activation of the receptor. Whereas the IC 50 value for a compound may vary between experiments depending on experimental conditions, (e.g. substrate and enzyme concentrations) the K i is an absolute value.
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Substrate dissociation rate contributes to how large or small the enzyme velocity will be. [2] In the Michaelis-Menten model, the enzyme binds to the substrate yielding an enzyme substrate complex, which can either go backwards by dissociating or go forward by forming a product. [2] The dissociation rate constant is defined using K off. [2]