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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. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    The effects of temperature on enzyme activity. Top: increasing temperature increases the rate of reaction (Q10 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.

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many therapeutic drugs and poisons are enzyme inhibitors.

  5. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Human enzymes start to denature quickly at temperatures above 40 °C. Enzymes from thermophilic archaea found in the hot springs are stable up to 100 °C. [13] However, the idea of an "optimum" rate of an enzyme reaction is misleading, as the rate observed at any temperature is the product of two rates, the reaction rate and the denaturation rate.

  6. Turnover number - Wikipedia

    en.wikipedia.org/wiki/Turnover_number

    In chemistry, the term "turnover number" has two distinct meanings. 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 ]

  7. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    Further addition of substrate would not increase the rate, and the enzyme is said to be saturated. The Michaelis constant is not affected by the concentration or purity of an enzyme. [16] Its value depends both on the identity of the enzyme and that of the substrate, as well as conditions such as temperature and pH.

  8. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Enzyme inhibitors are molecules that reduce or abolish enzyme activity, while enzyme activators are molecules that increase the catalytic rate of enzymes. These interactions can be either reversible (i.e., removal of the inhibitor restores enzyme activity) or irreversible (i.e., the inhibitor permanently inactivates the enzyme).

  9. Hyperthermia - Wikipedia

    en.wikipedia.org/wiki/Hyperthermia

    The increase in body temperature that results from a breakdown in thermoregulation affects the body biochemically. Enzymes involved in metabolic pathways within the body such as cellular respiration fail to work effectively at higher temperatures, and further increases can lead them to denature , reducing their ability to catalyse essential ...