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  2. Substrate presentation - Wikipedia

    en.wikipedia.org/wiki/Substrate_presentation

    When the substrate is present within a lipid raft, sequestration leads to an increased concentration of the protein near the substrate. Conversely, if the substrate is excluded from a lipid raft, sequestration results in decreased interaction between the protein and the substrate, as seen with PLD2. Either the substrate of the enzyme can move.

  3. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    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.

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/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.

  5. 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.

  6. Competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Competitive_inhibition

    Increasing the substrate concentration would diminish the "competition" for the substrate to properly bind to the active site and allow a reaction to occur. [3] When the substrate is of higher concentration than the concentration of the competitive inhibitor, it is more probable that the substrate will come into contact with the enzyme's active ...

  7. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    The "effective concentration" is the concentration the reactant would have to be, free in solution, to experiences the same collisional frequency. Often such theoretical effective concentrations are unphysical and impossible to realize in reality – which is a testament to the great catalytic power of many enzymes, with massive rate increases ...

  8. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    The reaction changes from approximately first-order in substrate concentration at low concentrations to approximately zeroth order at high concentrations. At small values of the substrate concentration this approximates to a first-order dependence of the rate on the substrate concentration:

  9. Regulatory enzyme - Wikipedia

    en.wikipedia.org/wiki/Regulatory_enzyme

    A regulatory enzyme is an enzyme in a biochemical pathway which, through its responses to the presence of certain other biomolecules, regulates the pathway activity.This is usually done for pathways whose products may be needed in different amounts at different times, such as hormone production.

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