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  2. Q10 (temperature coefficient) - Wikipedia

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

    The Q 10 coefficient represents the degree of temperature dependence a muscle exhibits as measured by contraction rates. [2] A Q 10 of 1.0 indicates thermal independence of a muscle whereas an increasing Q 10 value indicates increasing thermal dependence. Values less than 1.0 indicate a negative or inverse thermal dependence, i.e., a decrease ...

  3. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA. Conservation of enzyme requires that [28] = where is now the total enzyme concentration. After combining the two expressions some straightforward algebra leads to the following expression for the concentration ...

  4. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    For a given enzyme concentration and for relatively low substrate concentrations, the reaction rate increases linearly with substrate concentration; the enzyme molecules are largely free to catalyse the reaction, and increasing substrate concentration means an increasing rate at which the enzyme and substrate molecules encounter one another.

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme activity. An enzyme's name is ... The rate of a reaction is dependent on the activation energy needed to form the transition state ... temperature, substrate ...

  6. Activation energy - Wikipedia

    en.wikipedia.org/wiki/Activation_energy

    In some reactions, K 1 decreases with temperature more rapidly than k 2 increases, so that k actually decreases with temperature corresponding to a negative observed activation energy. [16] [17] [18] An example is the oxidation of nitric oxide which is a termolecular reaction +.

  7. 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.

  8. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    Enzymes utilizing such cofactors include the PLP-dependent enzyme aspartate transaminase and the TPP-dependent enzyme pyruvate dehydrogenase. [ 22 ] [ 23 ] Rather than lowering the activation energy for a reaction pathway, covalent catalysis provides an alternative pathway for the reaction (via to the covalent intermediate) and so is distinct ...

  9. Proteinase K - Wikipedia

    en.wikipedia.org/wiki/Proteinase_K

    An elevation of the reaction temperature from 37 °C to 50–60 °C may increase the activity several times, like the addition of 0.5–1% sodium dodecyl sulfate (SDS) or Guanidinium chloride (3 M), Guanidinium thiocyanate (1 M) and urea (4 M) [disputed (for: no source cited for temperature) – discuss]. The above-mentioned conditions enhance ...