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Substrates bind to enzymes at a specific location called the active site through a process known as enzyme-substrate complex formation.
Enzymes are biological catalysts that speed up chemical reactions in the body. They are proteins with a unique three-dimensional structure, which includes a specific area known as the active site. The active site is where the substrate, the molecule upon which the enzyme acts, binds. This binding is a crucial step in the process of enzyme-catalysed reactions.
The binding of a substrate to an enzyme's active site is often likened to a 'lock and key' model. In this model, the enzyme (the lock) has a specific shape into which the substrate (the key) fits perfectly. This model emphasises the specificity of enzymes; each enzyme will only bind to a particular substrate or group of substrates with a complementary shape.
However, the 'lock and key' model is a simplification. A more accurate model is the 'induced fit' model. In this model, the enzyme changes shape slightly when the substrate binds, moulding itself around the substrate to ensure a tighter fit. This change in shape also helps to catalyse the reaction, as it can put strain on the bonds in the substrate, making it easier for them to break and the reaction to proceed.
The binding of the substrate to the enzyme is also influenced by other factors, such as temperature, pH, and the concentration of the substrate. These factors can affect the rate at which the substrate binds to the enzyme and the rate at which the reaction proceeds. For example, if the temperature is too high, the enzyme can denature, or lose its shape, which means it can no longer bind to the substrate. Similarly, if the pH is too low or too high, it can affect the shape of the enzyme and its ability to bind to the substrate.
In summary, substrates bind to enzymes at the active site, and this binding is influenced by the shape of the enzyme and the substrate, as well as other factors such as temperature, pH, and substrate concentration.
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