All enzymes have an "optimal" rate of activity at a specific pH, and this rate goes down below and above it.
Equilibrium chemistry is a concerned with systems in chemical equilibrium. The unifying principle is that the free energy of a system at equilibrium is the minimum possible, so that the slope of the free energy with respect to the reaction coordinate is zero. This principle, applied to mixtures at equilibrium provides a definition of an equilibrium constant. Applications include acid-base, host-guest, metal-complex, solubility, partition, chromatography and redox equilibria.
A chemical system is said to be in equilibrium when the quantities of the chemical entities involved do not and cannot change in time without the application of an external influence. In this sense a system in chemical equilibrium is in a stable state. The system at chemical equilibrium will be at a constant temperature, pressure (or volume) and composition. It will be insulated from exchange of heat with the surroundings, that is, it is a closed system. A change of temperature, pressure (or volume) constitutes an external influence and the equilibrium quantities will change as a result of such a change. If there is a possibility that the composition might change, but the rate of change is negligibly slow, the system is said to be in a metastable state. The equation of chemical equilibrium can be expressed symbolically as
Enzyme kinetics is the study of the chemical reactions that are catalysed by enzymes. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction is 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 an agonist might inhibit the enzyme.
Enzymes are usually protein molecules that manipulate other molecules — the enzymes' substrates. These target molecules bind to an enzyme's active site and are transformed into products through a series of steps known as the enzymatic mechanism. These mechanisms can be divided into single-substrate and multiple-substrate mechanisms. Kinetic studies on enzymes that only bind one substrate, such as triosephosphate isomerase, aim to measure the affinity with which the enzyme binds this substrate and the turnover rate. Some other examples of enzymes are phosphofructokinase and hexokinase, both of which are important for cellular respiration (glycolysis).
Enzyme assays are laboratory methods for measuring enzymatic activity. They are vital for the study of enzyme kinetics and enzyme inhibition.
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