When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Enzyme assays are laboratory procedures that measure the rate of enzyme reactions. Since enzymes are not consumed by the reactions they catalyse, enzyme assays usually follow changes in the concentration of either substrates or products to measure the rate of reaction. There are many methods of measurement.

  3. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    Further addition of substrate would not increase the rate, and the enzyme is said to be saturated. The Michaelis constant is not affected by the concentration or purity of an enzyme. [16] Its value depends both on the identity of the enzyme and that of the substrate, as well as conditions such as temperature and pH.

  4. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Increasing the substrate concentration increases the rate of reaction (enzyme activity). However, enzyme saturation limits reaction rates. An enzyme is saturated when the active sites of all the molecules are occupied most of the time. At the saturation point, the reaction will not speed up, no matter how much additional substrate is added.

  5. Reversible Michaelis–Menten kinetics - Wikipedia

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

    When used to model enzyme rates in vivo , for example, to model a metabolic pathway, this representation is inadequate because under these conditions product is present. As a result, when building computer models of metabolism [ 1 ] or other enzymatic processes, it is better to use the reversible form of the Michaelis–Menten equation.

  6. Transition state theory - Wikipedia

    en.wikipedia.org/wiki/Transition_state_theory

    Because enzymes typically increase the non-catalyzed reaction rate by factors of 10 6-10 26, and Michaelis complexes [clarification needed] often have dissociation constants in the range of 10 −3-10 −6 M, it is proposed that transition state complexes are bound with dissociation constants in the range of 10 −14 -10 −23 M. As substrate ...

  7. Reaction progress kinetic analysis - Wikipedia

    en.wikipedia.org/wiki/Reaction_progress_kinetic...

    Intercepting reactions lying above (faster rates at the same substrate concentration) the parent reactions on the rate vs. substrate concentration plot, are indicative of catalyst deactivation under reaction conditions; further experimentation is necessary to distinguish product inhibition from other forms of catalyst death. [2]

  8. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    Enzyme catalysis is the increase in the rate of a process by an "enzyme", a biological molecule. Most enzymes are proteins, and most such processes are chemical reactions. Most enzymes are proteins, and most such processes are chemical reactions.

  9. 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 ...