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  2. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    Enzyme catalysis is the increase in the rate of a process by an "enzyme", a biological molecule. Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, called the active site.

  3. Turnover number - Wikipedia

    en.wikipedia.org/wiki/Turnover_number

    In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1] For enzymes with a single active site, k cat is referred to as the catalytic constant. [2]

  4. 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.

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    In some enzymes, no amino acids are directly involved in catalysis; instead, the enzyme contains sites to bind and orient catalytic cofactors. [30] Enzyme structures may also contain allosteric sites where the binding of a small molecule causes a conformational change that increases or decreases activity. [31]

  6. Catalysis - Wikipedia

    en.wikipedia.org/wiki/Catalysis

    Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usually gaseous or liquid) as the reactant, or heterogeneous, whose components are not in the same phase. Enzymes and other biocatalysts are often considered as a third category. Catalysis is ubiquitous in chemical industry of all kinds. [6]

  7. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Enzyme kinetics cannot prove which modes of catalysis are used by an enzyme. However, some kinetic data can suggest possibilities to be examined by other techniques. For example, a ping–pong mechanism with burst-phase pre-steady-state kinetics would suggest covalent catalysis might be important in this enzyme's mechanism.

  8. Biocatalysis - Wikipedia

    en.wikipedia.org/wiki/Biocatalysis

    Regioselectivity and diastereoselectivity: Due to their complex three-dimensional structure, enzymes may distinguish between functional groups which are chemically situated in different regions of the substrate molecule. Enantioselectivity: Since almost all enzymes are made from L-amino acids, enzymes are chiral catalysts. As a consequence, any ...

  9. Katal - Wikipedia

    en.wikipedia.org/wiki/Katal

    The katal (symbol: kat) is that catalytic activity that will raise the rate of conversion by one mole per second in a specified assay system. [1] It is a unit of the International System of Units (SI) [1] used for quantifying the catalytic activity of enzymes (that is, measuring the enzymatic activity level in enzyme catalysis) and other catalysts.