Enzymes work on one substrate specifically. This is why there is millions of different types of enzymes to interact with all the molecules they need to metabolically and chemically react with.
Shape of an enzyme specifically shape of its active site determines enzyme specificity .
Enzyme specificity is mainly determined by the active site structure and the interactions between the enzyme and its substrate. The shape, charge, and chemical properties of the active site are crucial in determining which substrates can bind to the enzyme and undergo a catalyzed reaction. Additionally, enzymes undergo conformational changes upon substrate binding to further enhance specificity.
The size of the enzyme's active site would not contribute significantly to substrate specificity. Substrate specificity is typically determined by the shape, charge, and chemical properties of the active site that can properly bind to the substrate.
each enzyme has a specific substrate to which it binds through a definite active site and any other enzyme can not bind to it
enzyme specificity
Enzyme specificity .
What an enzyme does is based on its shape, therefore you would have to change it on a molecular level in order to alter its job.
Enzyme specificity ensures that the enzyme can bind to its specific substrate with high affinity, increasing the likelihood of the catalytic reaction taking place. This promotes enzyme activity by enhancing the efficiency of substrate recognition and conversion, leading to a more rapid and precise catalytic process.
Protein structure plays a key role in enzyme specificity by determining the shape and active site of the enzyme. The unique 3D structure of an enzyme's active site allows it to bind specific substrates with complementary shapes, leading to catalysis of specific chemical reactions. Any changes in the enzyme's structure can affect its ability to recognize and bind to its substrate, thereby impacting its specificity.
The unit of specificity constant is typically expressed in units of M^(-1)·s^(-1) since it represents the efficiency of an enzyme in converting substrate to product per unit time for a given substrate concentration. The lower the value of the specificity constant, the less efficient the enzyme is at converting substrate to product.
Enzymes exhibit different types of specificity, including substrate specificity (acting on a specific substrate), stereospecificity (acting on a specific stereoisomer), and regiospecificity (acting at a specific region of a substrate). For example, trypsin exhibits substrate specificity by cleaving peptide bonds after lysine or arginine residues, while lactase exhibits substrate specificity by hydrolyzing lactose.
The active site of an enzyme is a specific region where the substrate binds and undergoes a chemical reaction. It contains amino acid residues that interact with the substrate to facilitate the conversion of reactants into products. The shape and properties of the active site are crucial for enzyme specificity and catalytic activity.