Michaelis-Menten kinetics
Michaelis-Menten kinetics (pronunciation: mi-kae-lis men-ten ki-net-ics) is a model in biochemistry that describes how the rate of an enzyme-catalyzed reaction changes with varying concentrations of substrate. It is named after German biochemist Leonor Michaelis and Canadian physician Maud Menten who proposed the model in 1913.
Etymology
The term "Michaelis-Menten kinetics" is derived from the names of Leonor Michaelis and Maud Menten, who first proposed this model. The term "kinetics" comes from the Greek word "kinesis" meaning movement, referring to the study of rates of chemical processes.
Description
Michaelis-Menten kinetics is based on the Michaelis-Menten equation, which mathematically describes the rate of enzymatic reactions. In this model, an enzyme binds to a substrate to form an enzyme-substrate complex, which then either dissociates back into the enzyme and substrate or proceeds to form the product. The rate at which the product is formed is dependent on the concentration of the substrate.
Key Terms
- Enzyme: A protein that acts as a catalyst to bring about a specific biochemical reaction.
- Substrate: A molecule upon which an enzyme acts.
- Enzyme-Substrate Complex: A temporary molecule formed when an enzyme comes into perfect contact with its substrate.
- Product: The compounds that are formed when an enzyme acts on a substrate.
Related Terms
- Enzyme kinetics: The study of the chemical reactions that are catalyzed by enzymes.
- Catalyst: A substance that increases the rate of a chemical reaction without itself undergoing any permanent chemical change.
- Biochemical reaction: A chemical reaction that occurs inside the cells of living things.
See Also
External links
- Medical encyclopedia article on Michaelis-Menten kinetics
- Wikipedia's article - Michaelis-Menten kinetics
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