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  2. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    For a given enzyme concentration and for relatively low substrate concentrations, the reaction rate increases linearly with substrate concentration; the enzyme molecules are largely free to catalyse the reaction, and increasing substrate concentration means an increasing rate at which the enzyme and substrate molecules encounter one another.

  3. 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.

  4. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA. Conservation of enzyme requires that [28] = where is now the total enzyme concentration. After combining the two expressions some straightforward algebra leads to the following expression for the concentration ...

  5. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    They are classified according to the effect of the inhibitor on the V max (maximum reaction rate catalysed by the enzyme) and K m (the concentration of substrate resulting in half maximal enzyme activity) as the concentration of the enzyme's substrate is varied. [15] [16]

  6. Competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Competitive_inhibition

    Michaelis–Menten plot of the reaction velocity (v) against substrate concentration [S] of normal enzyme activity (1) compared to enzyme activity with a competitive inhibitor (2). Adding a competitive inhibitor to an enzymatic reaction increases the K m of the reaction, but the V max remains the same.

  7. IC50 - Wikipedia

    en.wikipedia.org/wiki/IC50

    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.

  8. Control coefficient (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Control_coefficient...

    For example, a drug, changes in enzyme expression etc. The advantage is that the control coefficient becomes independent of the applied perturbation. For control coefficients defined in terms of changes in enzyme expression, it is often assumed that the effect on the local rate by changes to the enzyme activity is proportional so that:

  9. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme activity. An enzyme's name is ... concentration required for an enzyme to reach one ... substrate and the inhibitor affect each other. The enzyme's function is ...