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  2. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes with this property are called catalytically perfect or kinetically perfect. Example of such enzymes are triose-phosphate isomerase, carbonic anhydrase, acetylcholinesterase, catalase, fumarase, β-lactamase, and superoxide dismutase. [1]: 8.4.2 The turnover of such enzymes can reach several million reactions per second.

  3. 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 ...

  4. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    As shown on the right, enzymes with a substituted-enzyme mechanism can exist in two states, E and a chemically modified form of the enzyme E*; this modified enzyme is known as an intermediate. In such mechanisms, substrate A binds, changes the enzyme to E* by, for example, transferring a chemical group to the active site, and is then released.

  5. Cytochrome P450 (individual enzymes) - Wikipedia

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

    The fluctuation in the amount of CYP450 enzymes (CYP1A2, CYP2C8, CYP2C9, CYP2C19, CYP2D6, CYP3A4, and CYP3A5) in phase 1 (detoxification) can have varying effects on individuals, as genetic expression varies from person to person. This variation is due to the enzyme's genetic polymorphism, which leads to variability in its function and expression.

  6. 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 ...

  7. Category:Enzymes - Wikipedia

    en.wikipedia.org/wiki/Category:Enzymes

    EC 4 Lyases: cleave various bonds by means other than hydrolysis and oxidation; EC 5 Isomerases: catalyze isomerization changes within a single molecule; EC 6 Ligases: join two molecules with covalent bonds; For a list of enzymes currently sorted in this category, see List of enzymes

  8. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Since most enzymes have an optimum pH of 6 to 7, the amino acids in the side chain usually have a pK a of 4~10. Candidate include aspartate , glutamate , histidine , cysteine . These acids and bases can stabilise the nucleophile or electrophile formed during the catalysis by providing positive and negative charges.

  9. 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]