Enzymes are protein molecules that act as catalysts to break down substances living thing need to sustain life. Most chemical reactions are too lengthy to do this on their own; even in the cases of relatively thermodynamically favored reactions like that of the oxidation of a sugar. An example of this is the oxidation of glucose to produce water, carbon dioxide and energy. Glucose on its own can remain exposed to air for years without any appreciable oxidation. Nevertheless, it is one of the substances most quickly broken down and absorbed in the human body due to the digestive system’s ability to produce the appropriate enzymes to oxidize and utilize this substance to produce energy. .
Early in the twentieth century, Victor Henri discovered the binding interactions between enzymes and substrates. His work investigated the kinetics of the enzymes, the saccharase, which splits saccharose into glucose and fructose. Michaelis and Menten furthered his work in the course of their investigation regarding the kinetics of the enzymes, the saccharase, and the process that splits saccharose into glucose and fructose. . Michaelis-Menten kinetics is now one of the best know and broadly accepted models of enzyme kinetics.
Leonor Michaelis and Maud Menten first proposed in 1913 the mathematical model of the reaction involving binding an enzyme E binding to a substrate S to form a complex ES. This is then converted into a product P and the enzyme. (For the formula for this please see the full work up presented by Professor W. R. Salzman, on his professional pages in the University of Arizona as it appears in Appendix A attached hereto). . This equation denotes the process, the rate constants and double arrows between S and ES represent that the enzyme-substrate binding is reversible.
Since ideal conditions do not always exist, the Michaelis and Menten further defined their analysis of the process to allow for those situations where the enzyme concentration is much less than the substrate concentration. In that event, the product formation rate slows and increases based upon the degree of substrate concentration, .
The situation can also exist where there is more enzyme than substrate available. In this event, the formation process is once again governed by imbalance. However, it is increasing or decreasing amounts of enzyme that will alter the rate and success of the reaction. .
The amounts and concentration of enzyme and substrate ore not the only factors to consider when computing potential formulation times and success rates for enzyme kinetics using the Michaelis-Menten process, or when using any other formulation equations. Temperature variables also can greatly affect the speed and success rate of the kinetic process. Since enzymes are associated with living entities and their metabolic processes, the enzyme interaction is generally skewed so as to produce the greatest amount of product when it is most needed to sustain life. The temperature range for optimal performance depends upon the particular temperature range in which these conditions exist.
Another factor that influences this process is the pH balance under which the synthesis takes place. Once again, this tends to be biologically linked to the organism that utilizes the particular enzyme and substrate to produce life-sustaining substances. In this situation, the defining factor is not to produce maximum product at the greatest time of need based upon cellular and physical activity. In situations involving the pH factor, the reaction speed and success rate is based upon the optimal environmental conditions for the living organism dependent upon the interaction. Under certain living conditions, it may be more important for the organism to focus its resources elsewhere in order to sustain life. Because of this, both temperature and pH based enzyme and substrate reactions’ rate of speed tend to reflect the best life sustaining conditions for the host organism and therefore increase or slow dependent upon these variables. .
At times, there may also be other molecules that affect this process. This occurs most often when these molecules bind to the substrate in the receptor sites intended for the enzyme. However, there are also situations where molecules exist that attract the enzyme and bind to it instead of allowing it to bind to the substrate. This is not always a negative factor and sometimes can assist the host organism to maintain homeostasis. In situations where there is an excess of enzyme or substrate it may be beneficial to introduce binding molecules as a remedial procedure to reestablish a balance between enzyme and substrate and thereby optimize the metabolic processes.
Michaelis-Menten kinetics is now one of the best know and broadly accepted models of enzyme kinetics. Michaelis and Menten based their research on Victor Henri’s work from the early twentieth century regarding the binding interactions between enzymes and substrates in regards to kinetics of how saccharase, splits saccharose into glucose and fructose. Michaelis and Menten furthered this research when they conducted their investigation regarding the kinetics. They developed specific mathematic formulas to define the parameters regarding the interactions between enzymes and substrates that can also sometimes apply to other chemical interactions and relationships as well.
Nicolaas, S., & Trombeta, A. (1994). Biography of Victor Henri. L'Année Psychologique, 385 - 402. Retrieved from Who Named It?
Salzman, W. R. (2004, 04 09). Enzyme Kinetics. Retrieved from University of Arizona: http://chem.arizona.edu/~salzmanr/480a/480ants/enzymekn/enzymekn.html