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  2. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    In 1926, James B. Sumner showed that the enzyme urease was a pure protein and crystallized it; he did likewise for the enzyme catalase in 1937. The conclusion that pure proteins can be enzymes was definitively demonstrated by John Howard Northrop and Wendell Meredith Stanley, who worked on the digestive enzymes pepsin (1930), trypsin and ...

  3. 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).

  4. List of proteins - Wikipedia

    en.wikipedia.org/wiki/List_of_proteins

    Enzymes classified according to their Enzyme Commission number (EC). Note that strictly speaking, an EC number corresponds to the reaction the enzyme catalyzes, not the protein per se. However each EC number has been mapped to one or more specific proteins. List of enzymes; EC 1: Oxidoreductases; EC 2: Transferases; EC 3: Hydrolases; EC 4: Lyases

  5. Metabolic pathway - Wikipedia

    en.wikipedia.org/wiki/Metabolic_pathway

    An example of a coupled reaction is the phosphorylation of fructose-6-phosphate to form the intermediate fructose-1,6-bisphosphate by the enzyme phosphofructokinase accompanied by the hydrolysis of ATP in the pathway of glycolysis. The resulting chemical reaction within the metabolic pathway is highly thermodynamically favorable and, as a ...

  6. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    Modified amino acids are sometimes observed in proteins; this is usually the result of enzymatic modification after translation (protein synthesis). For example, phosphorylation of serine by kinases and dephosphorylation by phosphatases is an important control mechanism in the cell cycle. Only two amino acids other than the standard twenty are ...

  7. 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.

  8. Flavin-containing monooxygenase - Wikipedia

    en.wikipedia.org/wiki/Flavin-containing_mono...

    The general function of these enzymes is to metabolise xenobiotics. [16] Hence, they are considered to be xenobiotic detoxication catalysts. These proteins catalyze the oxygenation of multiple heteroatom-containing compounds that are present in our diet, such as amine-, sulfide-, phosphorus-, and other nucleophilic heteroatom-containing compounds.

  9. Category:Enzymes by function - Wikipedia

    en.wikipedia.org/wiki/Category:Enzymes_by_function

    Enzymes appear in this category according to the EC number classification: EC 1 Oxidoreductases: catalyze oxidation/reduction reactions; EC 2 Transferases: transfer a functional group (e.g. a methyl or phosphate group) EC 3 Hydrolases: catalyze the hydrolysis of various bonds; EC 4 Lyases: cleave various bonds by means other than hydrolysis and ...