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  2. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme denaturation is normally linked to temperatures above a species' normal level; as a result, enzymes from bacteria living in volcanic environments such as hot springs are prized by industrial users for their ability to function at high temperatures, allowing enzyme-catalysed reactions to be operated at a very high rate.

  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). One of the components is ...

  4. Translocase - Wikipedia

    en.wikipedia.org/wiki/Translocase

    Several of these involve the hydrolysis of ATP and had been previously classified as ATPases (EC 3.6.3.-), although the hydrolytic reaction is not their primary function. In August 2018, the International Union of Biochemistry and Molecular Biology classified these enzymes under a new enzyme class (EC) of translocases (EC 7). [2]

  5. 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 ...

  6. Exoenzyme - Wikipedia

    en.wikipedia.org/wiki/Exoenzyme

    An exoenzyme, or extracellular enzyme, is an enzyme that is secreted by a cell and functions outside that cell. Exoenzymes are produced by both prokaryotic and eukaryotic cells and have been shown to be a crucial component of many biological processes. Most often these enzymes are involved in the breakdown of larger macromolecules.

  7. 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 ...

  8. 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 ...

  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]