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  2. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Other list of enzymes. List of EC numbers (EC 5) List of EC numbers (EC 6) This page was last edited on 10 September 2024, at 18:48 (UTC). Text is available under the ...

  3. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    An enzyme's activity decreases markedly outside its optimal temperature and pH, and many enzymes are (permanently) denatured when exposed to excessive heat, losing their structure and catalytic properties. Some enzymes are used commercially, for example, in the synthesis of antibiotics.

  4. 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.

  5. Cytochrome P450 (individual enzymes) - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_P450...

    For example, bioactive compounds found in grapefruit juice and some other fruit juices, including bergamottin, dihydroxybergamottin, and paradicin-A, have been found to inhibit CYP3A4-mediated metabolism of certain medications, leading to increased bioavailability and, thus, the strong possibility of overdosing. [12]

  6. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    Both are used by enzymes and have been evolutionarily chosen to minimize the activation energy of the reaction. Enzymes that are saturated, that is, have a high affinity substrate binding, require differential binding to reduce the energy of activation, whereas small substrate unbound enzymes may use either differential or uniform binding. [4]

  7. Regulatory enzyme - Wikipedia

    en.wikipedia.org/wiki/Regulatory_enzyme

    Properties. Allosteric enzymes are generally larger in mass than other enzymes. Different from having a single subunit enzyme, in this case they are composed of multiple subunits, which contain active sites and regulatory molecule binding sites. They present a special kinetics: the cooperation. In here, configuration changes in each chain of ...

  8. Hydrolase - Wikipedia

    en.wikipedia.org/wiki/Hydrolase

    Hydrolase enzymes are important for the body because they have degradative properties. In lipids, lipases contribute to the breakdown of fats and lipoproteins and other larger molecules into smaller molecules like fatty acids and glycerol. Fatty acids and other small molecules are used for synthesis and as a source of energy. [1]

  9. Isozyme - Wikipedia

    en.wikipedia.org/wiki/Isozyme

    In biochemistry, isozymes (also known as isoenzymes or more generally as multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. Isozymes usually have different kinetic parameters (e.g. different K M values), or are regulated differently.