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  2. Q10 (temperature coefficient) - Wikipedia

    en.wikipedia.org/wiki/Q10_(temperature_coefficient)

    The effects of temperature on enzyme activity. Top - increasing temperature increases the rate of reaction (Q 10 coefficient). Middle - the fraction of folded and functional enzyme decreases above its denaturation temperature. Bottom - consequently, an enzyme's optimal rate of reaction is at an intermediate temperature.

  3. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    As shown on the right, enzymes with a substituted-enzyme mechanism can exist in two states, E and a chemically modified form of the enzyme E*; this modified enzyme is known as an intermediate. In such mechanisms, substrate A binds, changes the enzyme to E* by, for example, transferring a chemical group to the active site, and is then released.

  4. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Enzyme activity as given in katal generally refers to that of the assumed natural target substrate of the enzyme. Enzyme activity can also be given as that of certain standardized substrates, such as gelatin, then measured in gelatin digesting units (GDU), or milk proteins, then measured in milk clotting units (MCU). The units GDU and MCU are ...

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme activity. An enzyme's name is often derived from its substrate or the chemical reaction it catalyzes, with the word ending in -ase. [1]: 8.1.3 Examples are lactase, alcohol dehydrogenase and DNA polymerase. Different enzymes that catalyze the same chemical reaction are called isozymes. [1]: 10.3

  6. Taq polymerase - Wikipedia

    en.wikipedia.org/wiki/Taq_polymerase

    At temperatures above 90 °C, Taq demonstrates very little or no activity at all, but the enzyme itself does not denature and remains intact. [5] Presence of certain ions in the reaction vessel also affects specific activity of the enzyme. Small amounts of potassium chloride (KCl) and magnesium ion (Mg 2+) promote Taq's enzymatic activity.

  7. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    A decade before Michaelis and Menten, Victor Henri found that enzyme reactions could be explained by assuming a binding interaction between the enzyme and the substrate. [11] His work was taken up by Michaelis and Menten, who investigated the kinetics of invertase, an enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose. [12]

  8. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    Instrumental set up: A typical temperature ramp rates range from 0.1 to 10 °C/min but generally in the range of 1 °C/min. The fluorescence in each well is measured at regular intervals, 0.2–1 °C/image, over a temperature range spanning the typical protein unfolding temperatures of 25–95 °C. [19]

  9. Extremozyme - Wikipedia

    en.wikipedia.org/wiki/Extremozyme

    An extremozyme is an enzyme, often created by archaea, which are known prokaryotic extremophiles that can function under extreme environments. Examples of such are those in highly acidic/basic conditions, high/low temperatures, high salinity, or other factors, that would otherwise denature typical enzymes (e.g. catalase, rubisco, carbonic anhydrase). [1]