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  2. 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. Within the enzyme, generally catalysis occurs at a localized site, called the active site.

  3. Catalysis - Wikipedia

    en.wikipedia.org/wiki/Catalysis

    Biocatalysts can be thought of as an intermediate between homogeneous and heterogeneous catalysts, although strictly speaking soluble enzymes are homogeneous catalysts and membrane-bound enzymes are heterogeneous. Several factors affect the activity of enzymes (and other catalysts) including temperature, pH, the concentration of enzymes ...

  4. Biocatalysis - Wikipedia

    en.wikipedia.org/wiki/Biocatalysis

    Regioselectivity and diastereoselectivity: Due to their complex three-dimensional structure, enzymes may distinguish between functional groups which are chemically situated in different regions of the substrate molecule. Enantioselectivity: Since almost all enzymes are made from L-amino acids, enzymes are chiral catalysts. As a consequence, any ...

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many therapeutic drugs and poisons are enzyme inhibitors.

  6. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The main difference between ribozymes and enzymes is that RNA catalysts are composed of nucleotides, whereas enzymes are composed of amino acids. Ribozymes also perform a more limited set of reactions, although their reaction mechanisms and kinetics can be analysed and classified by the same methods.

  7. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    An important factor in drug design is the strength of binding between the active site and an enzyme inhibitor. [20] If the enzyme found in bacteria is significantly different from the human enzyme then an inhibitor can be designed against that particular bacterium without harming the human enzyme.

  8. Activation energy - Wikipedia

    en.wikipedia.org/wiki/Activation_energy

    A catalyst is able to reduce the activation energy by forming a transition state in a more favorable manner. Catalysts, by nature, create a more "comfortable" fit for the substrate of a reaction to progress to a transition state. This is possible due to a release of energy that occurs when the substrate binds to the active site of a catalyst ...

  9. Ribozyme - Wikipedia

    en.wikipedia.org/wiki/Ribozyme

    The techniques used to create artificial ribozymes involve directed evolution. This approach takes advantage of RNA's dual nature as both a catalyst and an informational polymer, making it easy for an investigator to produce vast populations of RNA catalysts using polymerase enzymes.