The “lock-and-key” theory is a fundamental concept in molecular biology that explains the specificity of enzymes and their substrates. The theory was first proposed by Emil Fischer in 1894 and has since become an essential basis for understanding the processes of biological catalysis (Berg, Tymoczko, & Stryer, 2018). The theory states that an enzyme and its substrate must fit together like a lock and key, in which the shape of the enzyme’s active site matches the shape of the substrate’s functional group (Berg et al., 2018). This shape complementarity allows the enzyme to bind to the substrate and catalyze the reaction (Berg et al., 2018).
The theory has been supported by numerous experiments, including x-ray crystallography and mutagenesis studies. X-ray crystallography is a technique used to determine the three-dimensional structure of molecules, which has been used to visualize the interactions between enzymes and their substrates (Berg et al., 2018). Mutagenesis studies involve the alteration of an enzyme’s sequence, which can be used to identify the specific amino acid residues that are involved in binding (Berg et al., 2018). Together, these studies have provided evidence that enzymes and their substrates interact through a lock-and-key mechanism.
The lock-and-key theory has also been applied to other systems, such as the binding of hormones to their receptors. Hormones are chemical messengers that bind to receptors on the surface of target cells, and this binding is mediated by a lock-and-key mechanism (Berg et al., 2018). In this system, the hormone acts as the key and the receptor acts as the lock, and the shape complementarity between the two allows the hormone to bind to and activate the receptor (Berg et al., 2018).
The lock-and-key theory is a fundamental concept in molecular biology that explains the specificity of enzymes and their substrates, as well as other systems such as the binding of hormones to their receptors. This theory has been supported by numerous experiments, including x-ray crystallography and mutagenesis studies, and it is an essential basis for understanding the processes of biological catalysis.
References
Berg, J. M., Tymoczko, J. L., & Stryer, L. (2018). Biochemistry (8th ed.). New York, NY: W. H. Freeman.