Induced fit is a term commonly used in biochemistry to describe the interaction between an enzyme and its substrate. The correct spelling of this word is represented phonetically as /ɪnˈdjuːst fɪt/. The word induced is pronounced with a short "i" sound before the "n" and a long "u" sound before the "d". Fit is pronounced with a short "i" sound followed by the "t" sound. Understanding the accurate phonetic transcription of induced fit is necessary to effectively communicate about biochemical reactions involving this process.
Induced fit is a concept in biochemistry that describes the dynamic process by which an enzyme undergoes conformational changes upon interaction with its substrate, in order to enhance the binding affinity and catalytic activity of the enzyme.
When a substrate molecule approaches and binds to the active site of an enzyme, the enzyme undergoes structural adjustments or conformational changes to accommodate the substrate. This induced fit causes the enzyme's active site to more closely resemble the shape and chemical properties of the substrate, allowing for optimal complementarity and interaction. In this process, the binding of the substrate induces a change in the enzyme's shape, which in turn leads to the formation of specific enzyme-substrate interactions.
The induced fit model is in contrast to the lock and key model, another conceptual idea of enzyme-substrate interactions. The lock and key model suggests that the active site of an enzyme is rigid and static, matching the shape of the substrate perfectly in a pre-existing manner. However, the induced fit model recognizes the dynamic nature of enzymes, indicating that the binding event itself causes conformational changes that enable optimal binding and catalysis.
This induced fit mechanism allows for greater catalytic efficiency and specificity in enzyme-substrate interactions. As the substrate binds to the enzyme, the induced conformational changes optimize the alignment and positioning of active site residues, facilitating chemical reactions with greater efficiency and specificity. The induced fit model is widely accepted as a crucial aspect of enzyme function and is fundamental to understanding how enzymes carry out their biological roles.
The term "induced fit" was coined by the biochemist Daniel Koshland in 1958. The etymology of the word comes from the combination of two key words: "induced" and "fit".
- "Induced" refers to the idea that the binding of a substrate (or ligand) to an enzyme induces a conformational change in the enzyme's active site. This conformational change is caused by specific interactions and forces between the enzyme and the substrate.
- "Fit" refers to the complementary matching between the substrate and the active site of the enzyme. The active site undergoes a conformational change to accommodate the substrate, creating an optimal fit for catalysis to occur.