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  2. 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.

  3. Enzyme unit - Wikipedia

    en.wikipedia.org/wiki/Enzyme_unit

    The enzyme unit, or international unit for enzyme (symbol U, sometimes also IU) is a unit of enzyme's catalytic activity. [1]1 U (μmol/min) is defined as the amount of the enzyme that catalyzes the conversion of one micro mole of substrate per minute under the specified conditions of the assay method.

  4. Control coefficient (biochemistry) - Wikipedia

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

    In biochemistry, control coefficients [1] are used to describe how much influence a given reaction step has on the flux or concentration of the species at steady state.This can be accomplished experimentally by changing the expression level of a given enzyme and measuring the resulting changes in flux and metabolite levels.

  5. 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.

  6. Katal - Wikipedia

    en.wikipedia.org/wiki/Katal

    The katal (symbol: kat) is that catalytic activity that will raise the rate of conversion by one mole per second in a specified assay system. [1] It is a unit of the International System of Units (SI) [1] used for quantifying the catalytic activity of enzymes (that is, measuring the enzymatic activity level in enzyme catalysis) and other catalysts.

  7. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme structures unfold when heated or exposed to chemical denaturants and this disruption to the structure typically causes a loss of activity. [27] Enzyme denaturation is normally linked to temperatures above a species' normal level; as a result, enzymes from bacteria living in volcanic environments such as hot springs are prized by ...

  8. Summation theorems (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Summation_theorems...

    Moreover, Kacser and Burns [13] suggested that since the flux–enzyme relationship is somewhat hyperbolic, and that for most enzymes, the wild-type diploid level of enzyme activity occurs where the curve is reaching a point in the curve where changes have little effect, then since a heterozygote of the wild-type with a null mutant will have ...

  9. Metabolic control analysis - Wikipedia

    en.wikipedia.org/wiki/Metabolic_control_analysis

    A control coefficient [10] [11] [12] measures the relative steady state change in a system variable, e.g. pathway flux (J) or metabolite concentration (S), in response to a relative change in a parameter, e.g. enzyme activity or the steady-state rate of step . The two main control coefficients are the flux and concentration control coefficients.