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  2. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    An important goal of measuring enzyme kinetics is to determine the chemical mechanism of an enzyme reaction, i.e., the sequence of chemical steps that transform substrate into product. The kinetic approaches discussed above will show at what rates intermediates are formed and inter-converted, but they cannot identify exactly what these ...

  3. Reversible Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Reversible_Michaelis...

    Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. The study of how fast an enzyme can transform a substrate into a product is called enzyme kinetics. The rate of reaction of many chemical reactions shows a linear response as function of the concentration of substrate molecules.

  4. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    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]

  5. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    The enzyme involved in this reaction is called invertase, and it is the enzyme the kinetics of which have been supported by Michaelis and Menten to be revolutionary for the kinetics of other enzymes. While expressing the rate of the reaction studied, they derived an equation that described the rate in a way which suggested that it is mostly ...

  6. Isocitrate dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Isocitrate_dehydrogenase

    In the provided figure, the first box shows the overall isocitrate dehydrogenase reaction. The necessary reactants for this enzyme mechanism are isocitrate, NAD + /NADP +, and Mn 2+ or Mg 2+. The products of the reaction are alpha-ketoglutarate, carbon dioxide, and NADH + H + /NADPH + H +. [10] Water molecules help to deprotonate the oxygen ...

  7. Stopped-flow - Wikipedia

    en.wikipedia.org/wiki/Stopped-flow

    Stopped-flow spectrometry enables the solution-phase study of chemical kinetics for fast reactions, typically with half-lives in the millisecond range. Initially, it was primarily used for investigating enzyme-catalyzed reactions but quickly became a staple in biochemistry, biophysics, and chemistry laboratories for tracking rapid chemical ...

  8. Cofactor (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Cofactor_(biochemistry)

    The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.. A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction).

  9. Chemical kinetics - Wikipedia

    en.wikipedia.org/wiki/Chemical_kinetics

    Chemical kinetics, also known as reaction kinetics, is the branch of physical chemistry that is concerned with understanding the rates of chemical reactions. It is different from chemical thermodynamics , which deals with the direction in which a reaction occurs but in itself tells nothing about its rate.