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  2. Phosphoribulokinase - Wikipedia

    en.wikipedia.org/wiki/Phosphoribulokinase

    Phosphoribulokinase (PRK) (EC 2.7.1.19) is an essential photosynthetic enzyme that catalyzes the ATP-dependent phosphorylation of ribulose 5-phosphate (RuP) into ribulose 1,5-bisphosphate (RuBP), both intermediates in the Calvin Cycle.

  3. Fructose 1,6-bisphosphatase - Wikipedia

    en.wikipedia.org/wiki/Fructose_1,6-bisphosphatase

    This adaptation allows enzymes such as FBPase and fructose-1,6-bisphosphate aldolase to track intracellular pH changes in hibernating animals and match their activity ranges to these shifts. [14] Aldolase also complements the activity of FBPase in anoxic conditions (discussed above) by increasing glycolytic output while FBPase inhibition ...

  4. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Most enzymes are sensitive to pH and have specific ranges of activity. All have an optimum pH. The pH can stop enzyme activity by denaturating (altering) the three-dimensional shape of the enzyme by breaking ionic, and hydrogen bonds. Most enzymes function between a pH of 6 and 8; however pepsin in the stomach works best at a pH of 2 and ...

  5. 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.

  6. Intracellular pH - Wikipedia

    en.wikipedia.org/wiki/Intracellular_pH

    Intracellular pH (pH i) is the measure of the acidity or basicity (i.e., pH) of intracellular fluid. The pH i plays a critical role in membrane transport and other intracellular processes. In an environment with the improper pH i , biological cells may have compromised function.

  7. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier (inhibitor or activator) might affect the ...

  8. PNGase F - Wikipedia

    en.wikipedia.org/wiki/PNGase_F

    The optimal pH for enzyme activity is 8.6. However, the activity is stable for a wide variety of conditions and reagents. PNGase F maintains 60% activity from pH 6.0 to pH 9.5. It is able to deglycosylate in the absence of denaturants, but needs extensive incubation and larger amounts of the enzyme to cleave native proteins. [1] [4] [5]

  9. Acid–base homeostasis - Wikipedia

    en.wikipedia.org/wiki/Acid–base_homeostasis

    An acid-base diagram for human plasma, showing the effects on the plasma pH when P CO 2 in mmHg or Standard Base Excess (SBE) occur in excess or are deficient in the plasma [23] Acid–base imbalance occurs when a significant insult causes the blood pH to shift out of the normal range (7.32 to 7.42 [ 16 ] ).