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  2. Viral neuraminidase - Wikipedia

    en.wikipedia.org/wiki/Viral_neuraminidase

    Neuraminidase enzymes can have endo- or exo-glycosidase activity, and are classified as EC 3.2.1.29 (endo-neuraminidase) [9] and EC 3.2.1.18 (exo-neuraminidases). [10] In general, mammalian sialic acid residues are at terminal positions (non-reducing end) in complex glycans, and so viral neuraminidases - which are exo- glycosidase enzymes - use ...

  3. Acetylcholinesterase - Wikipedia

    en.wikipedia.org/wiki/Acetylcholinesterase

    It is an enzyme that catalyzes the breakdown of acetylcholine and some other choline esters that function as neurotransmitters: acetylcholine + H 2 O = choline + acetate It is found at mainly neuromuscular junctions and in chemical synapses of the cholinergic type, where its activity serves to terminate cholinergic synaptic transmission .

  4. Lysosome - Wikipedia

    en.wikipedia.org/wiki/Lysosome

    The result was the same no matter how many times they repeated the estimation, and led to the conclusion that a membrane-like barrier limited the accessibility of the enzyme to its substrate, and that the enzymes were able to diffuse after a few days (and react with their substrate).

  5. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    The enzymes can also help to properly orient the ATP molecule, as well as the inositol group, to make the reaction proceed faster. Metal ions are often coordinated for this purpose. [24] Mechanism of phosphatidylinositol-3 kinase. ATP and phosphatidylinositol react to form phosphatidylinositol-3-phosphate and ADP, with the help of general base ...

  6. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    If the answer is yes then the reaction is the general type. 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 ...

  7. Protease - Wikipedia

    en.wikipedia.org/wiki/Protease

    Ribbon diagram of a protease (TEV protease) complexed with its peptide substrate in black with catalytic residues in red.(. A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2]

  8. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    Biosynthesis, i.e., chemical synthesis occurring in biological contexts, is a term most often referring to multi-step, enzyme-catalyzed processes where chemical substances absorbed as nutrients (or previously converted through biosynthesis) serve as enzyme substrates, with conversion by the living organism either into simpler or more complex ...

  9. Carbonic anhydrase - Wikipedia

    en.wikipedia.org/wiki/Carbonic_anhydrase

    An enzyme is a substance that acts as a catalyst in living organisms which helps to speed up chemical reactions. [12] Carbonic anhydrase is one important enzyme that is found in red blood cells, gastric mucosa, pancreatic cells, and even renal tubules. It was discovered in the year 1932 and it has been categorized into three general classes. [13]