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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 activator - Wikipedia

    en.wikipedia.org/wiki/Enzyme_activator

    Hexokinase-I (HK-I) is an enzyme activator because it draws glucose into the glycolysis pathway. Its function is to phosphorylate glucose releasing glucose-6-phosphate (G6P) as the product. HK-I not only signals the activation of glucose into glycolysis but also maintains a low glucose concentration to facilitate glucose diffusion into the cell.

  4. Endoenzyme - Wikipedia

    en.wikipedia.org/wiki/Endoenzyme

    An endoenzyme, or intracellular enzyme, is an enzyme that functions within the cell in which it was produced. [1] Because the majority of enzymes fall within this category, the term is used primarily to differentiate a specific enzyme from an exoenzyme. It is possible for a single enzyme to have both endoenzymatic and exoenzymatic functions ...

  5. Isomerase - Wikipedia

    en.wikipedia.org/wiki/Isomerase

    The enzyme's active site contains two Asp residues. After the substrate binds to the enzyme, the first Asp deprotonates the third carbon from one side of the molecule. This leaves a planar sp 2-hybridized intermediate. The second Asp is located on the opposite side of the active side and it protonates the molecule, effectively adding a proton ...

  6. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    Dihydroxyacetone kinase in complex with a non-hydrolyzable ATP analog (AMP-PNP). Coordinates from PDB ID:1UN9. [1]In biochemistry, a kinase (/ ˈ k aɪ n eɪ s, ˈ k ɪ n eɪ s,-eɪ z /) [2] is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates.

  7. Isozyme - Wikipedia

    en.wikipedia.org/wiki/Isozyme

    All the proteins from the tissue are present in the gel, so that individual enzymes must be identified using an assay that links their function to a staining reaction. For example, detection can be based on the localised precipitation of soluble indicator dyes such as tetrazolium salts which become insoluble when they are reduced by cofactors ...

  8. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Different proteins are degraded at different rates. Abnormal proteins are quickly degraded, whereas the rate of degradation of normal proteins may vary widely depending on their functions. Enzymes at important metabolic control points may be degraded much faster than those enzymes whose activity is largely constant under all physiological ...

  9. Phosphatase - Wikipedia

    en.wikipedia.org/wiki/Phosphatase

    Because a phosphatase enzyme catalyzes the hydrolysis of its substrate, it is a subcategory of hydrolases. [1] Phosphatase enzymes are essential to many biological functions, because phosphorylation (e.g. by protein kinases) and dephosphorylation (by phosphatases) serve diverse roles in cellular regulation and signaling. [2]