enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  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

    Another useful constant is k cat, also called the turnover number, which is the number of substrate molecules handled by one active site per second. [1]: 8.4 The efficiency of an enzyme can be expressed in terms of k cat /K m.

  4. 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.

  5. Enzyme Commission number - Wikipedia

    en.wikipedia.org/wiki/Enzyme_Commission_number

    The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. [1] As a system of enzyme nomenclature, every EC number is associated with a recommended name for the corresponding enzyme-catalyzed reaction. EC numbers do not specify enzymes but enzyme-catalyzed reactions.

  6. Metabolic pathway - Wikipedia

    en.wikipedia.org/wiki/Metabolic_pathway

    The reactants, products, and intermediates of an enzymatic reaction are known as metabolites, which are modified by a sequence of chemical reactions catalyzed by enzymes. [1]: 26 In most cases of a metabolic pathway, the product of one enzyme acts as the substrate for the next. However, side products are considered waste and removed from the cell.

  7. Affinity label - Wikipedia

    en.wikipedia.org/wiki/Affinity_label

    The hallmark of an affinity label is the use of a targeting moiety to specifically and reversibly deliver a weakly reactive group to the enzyme that irreversibly binds to an amino acid residue. The targeting portion of the label often resembles the enzyme's natural substrate so that a similar mode of noncovalent binding is used prior to the ...

  8. Nitrogenase - Wikipedia

    en.wikipedia.org/wiki/Nitrogenase

    Nitrogenase is an enzyme responsible for catalyzing nitrogen fixation, which is the reduction of nitrogen (N 2) to ammonia (NH 3) and a process vital to sustaining life on Earth. [9] There are three types of nitrogenase found in various nitrogen-fixing bacteria: molybdenum (Mo) nitrogenase, vanadium (V) nitrogenase , and iron-only (Fe ...

  9. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    A sulfur nucleophile improved the enzymes transferase activity (sometimes called subtiligase). Selenium and tellurium nucleophiles converted the enzyme into an oxidoreductase . [ 51 ] [ 52 ] When the nucleophile of TEV protease was converted from cysteine to serine, it protease activity was strongly reduced, but was able to be restored by ...