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  2. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...

  3. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    The major contribution of Michaelis and Menten was to think of enzyme reactions in two stages. ... Enzymes with this property are called catalytically perfect or ...

  4. 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 ...

  5. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    A decade before Michaelis and Menten, Victor Henri found that enzyme reactions could be explained by assuming a binding interaction between the enzyme and the substrate. [11] His work was taken up by Michaelis and Menten, who investigated the kinetics of invertase, an enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose. [12]

  6. Cytochrome P450 - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_P450

    Depending on the substrate and enzyme involved, P450 enzymes can catalyze any of a wide variety of reactions. A hypothetical hydroxylation is illustrated. After the hydroxylated product has been released from the active site, the enzyme returns to its original state, with a water molecule returning to occupy the distal coordination position of ...

  7. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The two important properties of enzyme kinetics are how easily the enzyme can be saturated with a substrate, and the maximum rate it can achieve. Knowing these properties suggests what an enzyme might do in the cell and can show how the enzyme will respond to changes in these conditions.

  8. Cytochrome P450 (individual enzymes) - Wikipedia

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

    P450s are the major enzymes involved in drug metabolism, accounting for about 75% of the total metabolism. [7] Most drugs undergo deactivation by P450s, either directly or by facilitated excretion from the body. However, many substances are bioactivated by P450s to form their active compounds like the antiplatelet drug clopidogrel and the ...

  9. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Organisation of enzyme structure and lysozyme example. Binding sites in blue, catalytic site in red and peptidoglycan substrate in black. (In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.