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  2. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier (inhibitor or activator) might affect the rate. An enzyme (E) is a protein molecule that serves as a biological catalyst to facilitate and accelerate a chemical ...

  3. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Factors affecting enzyme activity As enzymes are made up of proteins, their actions are sensitive to change in many physio chemical factors such as pH, temperature, substrate concentration, etc. The following table shows pH optima for various enzymes.

  4. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Enzyme activity as given in katal generally refers to that of the assumed natural target substrate of the enzyme. Enzyme activity can also be given as that of certain standardized substrates, such as gelatin, then measured in gelatin digesting units (GDU), or milk proteins, then measured in milk clotting units (MCU). The units GDU and MCU are ...

  5. Flux (metabolism) - Wikipedia

    en.wikipedia.org/wiki/Flux_(metabolism)

    The activity of the enzyme catalysing the reaction; The properties of the enzyme; The metabolite concentration affecting enzyme activity. [5] Considering the above, the metabolic fluxes can be described as the ultimate representation of the cellular phenotype when expressed under certain conditions.

  6. 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.

  7. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.

  8. Cofactor (biochemistry) - Wikipedia

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

    Cosubstrates may be released from a protein at some point, and then rebind later. Both prosthetic groups and cosubstrates have the same function, which is to facilitate the reaction of enzymes and proteins. An inactive enzyme without the cofactor is called an apoenzyme, while the complete enzyme with cofactor is called a holoenzyme. [5] [page ...

  9. Enzyme activator - Wikipedia

    en.wikipedia.org/wiki/Enzyme_activator

    Enzyme activators are molecules that bind to enzymes and increase their activity. They are the opposite of enzyme inhibitors. These molecules are often involved in the allosteric regulation of enzymes in the control of metabolism. In some cases, when a substrate binds to one catalytic subunit of an enzyme, this can trigger an increase in the ...