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  2. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Although structure determines function, a novel enzymatic activity cannot yet be predicted from structure alone. [26] Enzyme structures unfold when heated or exposed to chemical denaturants and this disruption to the structure typically causes a loss of activity. [27]

  3. 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.

  4. 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 ...

  5. Lysosome - Wikipedia

    en.wikipedia.org/wiki/Lysosome

    They described this membrane-like barrier as a "saclike structure surrounded by a membrane and containing acid phosphatase." [18] It became clear that this enzyme from the cell fraction came from membranous fractions, which were definitely cell organelles, and in 1955 De Duve named them "lysosomes" to reflect their digestive properties. [19]

  6. Cytochrome P450 - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_P450

    Depending on the substrate and enzyme involved, P450 enzymes can catalyze any of a wide variety of reactions. A hypothetical hydroxylation is illustrated. After the hydroxylated product has been released from the active site, the enzyme returns to its original state, with a water molecule returning to occupy the distal coordination position of ...

  7. 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 ...

  8. Lysozyme - Wikipedia

    en.wikipedia.org/wiki/Lysozyme

    The enzyme functions by hydrolyzing glycosidic bonds in peptidoglycans. The enzyme can also break glycosidic bonds in chitin, although not as effectively as true chitinases. [10] Overview of the reaction catalysed by lysozyme. Lysozyme's active site binds the peptidoglycan molecule in the prominent cleft between its two domains.

  9. ATPase - Wikipedia

    en.wikipedia.org/wiki/ATPase

    Adenosine triphosphate Adenosine diphosphate Adenosine monophosphate. ATPases (EC 3.6.1.3, Adenosine 5'-TriPhosphatase, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, ATP hydrolase, complex V (mitochondrial electron transport), (Ca 2+ + Mg 2+)-ATPase, HCO 3 −-ATPase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP ...

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