Difference between an enzyme, an active site, and a substrate

Difference between an enzyme, an active site, and a substrate: Enzyme: Enzymes are proteins that act as catalysts in biological reactions. They accelerate chemical reactions by lowering the activation energy required for the reaction to occur. Enzymes remain unchanged after the reaction, allowing them to be reused. Active site: The active site is a specific region on the enzyme where the substrate binds. It is a highly specific and three-dimensional pocket that accommodates the substrate. The active site undergoes conformational changes upon substrate binding to facilitate the catalytic reaction. Substrate: A substrate refers to the molecule that interacts with the enzyme at the active site. It is the reactant molecule upon which the enzyme acts. Enzymes have high specificity for their substrates, meaning that each enzyme catalyzes a specific reaction by binding to a specific substrate or group of related substrates. Specific enzyme and mode of action - Trypsin: Trypsin is a digestive enzyme that plays a crucial role in protein digestion. It breaks down proteins into smaller peptides by hydrolyzing peptide bonds. Trypsin specifically cleaves peptide bonds on the carboxyl side of basic amino acids such as lysine and arginine. When ingested proteins reach the small intestine, trypsin is released by the pancreas as an inactive precursor called trypsinogen. Trypsinogen is activated by an enzyme called enterokinase, which removes a small peptide fragment, converting trypsinogen into its active form, trypsin. Once activated, trypsin binds to proteins and exhibits its proteolytic activity. It recognizes specific amino acid sequences containing basic residues (lysine and arginine) and cleaves the peptide bonds adjacent to these residues. The resulting peptides can be further broken down by other digestive enzymes into individual amino acids for absorption. Faulty or improper functioning of trypsin: When trypsin is faulty or not working properly, it can lead to various digestive disorders. One such disorder is hereditary pancreatitis, which is caused by mutations in the gene encoding for trypsinogen. These mutations render trypsinogen more prone to activation within the pancreas, leading to premature activation of trypsin and subsequent damage to pancreatic tissue. The excessive activation of trypsin leads to inflammation, tissue damage, and recurrent episodes of pancreatitis. Symptoms may include abdominal pain, nausea, vomiting, and malabsorption of nutrients due to impaired protein digestion. Furthermore, if trypsin is not produced or released in sufficient quantities, it can result in inadequate protein digestion. This can lead to malnutrition and deficiencies of essential amino acids necessary for growth, development, and overall health. In summary, trypsin is an enzyme involved in protein digestion, specifically breaking down proteins into smaller peptides. When faulty or not functioning properly, it can result in digestive disorders like hereditary pancreatitis or inadequate protein digestion, leading to malnutrition and other health complications.

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