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85. Mechanism Of Enzyme Action

𝐒𝐮𝐛𝐬𝐜𝐫𝐢𝐛𝐞 𝗙𝐨𝐫 𝗠𝐨𝐫𝐞 𝗜𝐧𝐟𝐨𝐫𝐦𝐚𝐭𝐢𝐨𝐧 𝐨𝐧 𝗛𝐞𝐚𝐥𝐭𝐡 👩‍⚕‍ 𝐚𝐧𝐝 𝗠𝐞𝐝𝐢𝐜𝐢𝐧𝐞💉🩺💊 𝐘𝐨𝐮𝐭𝐮𝐛𝐞 :    / @draishwaryakelkar   📌𝗙𝗮𝗰𝗲𝗯𝗼𝗼𝗸 :   / draishwaryakelkar   📌𝗧𝘄𝗶𝘁𝘁𝗲𝗿:   / aishwayadr   📌𝗜𝗻𝘀𝘁𝗮𝗴𝗿𝗮𝗺 :   / clinical.learning   An enzyme attracts substrates to its active site, catalyzes the chemical reaction by which products are formed, and then allows the products to dissociate (separate from the enzyme surface). The combination formed by an enzyme and its substrates is called the enzyme–substrate complex. When two substrates and one enzyme are involved, the complex is called a ternary complex; one substrate and one enzyme are called a binary complex. The substrates are attracted to the active site by electrostatic and hydrophobic forces, which are called noncovalent bonds because they are physical attractions and not chemical bonds. As an example, assume two substrates (S1 and S2) bind to the active site of the enzyme during step 1 and react to form products (P1 and P2) during step 2. The products dissociate from the enzyme surface in step 3, releasing the enzyme. The enzyme, unchanged by the reaction, is able to react with additional substrate molecules in this manner many times per second to form products. The step in which the actual chemical transformation occurs is of great interest, and, although much is known about it, it is not yet fully understood. In general there are two types of enzymatic mechanisms, one in which a so-called covalent intermediate forms and one in which none forms. In the mechanism by which a covalent intermediate—i.e., an intermediate with a chemical bond between substrate and enzyme—forms, one substrate, B―X, for example, reacts with the group N on the enzyme surface to form an enzyme-B intermediate compound. The intermediate compound then reacts with the second substrate, Y, to form the products B―Y and X. Many enzymes catalyze reactions by this type of mechanism. Acetylcholinesterase is used as a specific example in the sequence described below. The two substrates (S1 and S2) for acetylcholinesterase are acetylcholine (i.e., B―X) and water (Y). After acetylcholine (B―X) binds to the enzyme surface, a chemical bond forms between the acetyl moiety (B) of acetylcholine and the group N (part of the amino acid serine) on the enzyme surface. The result of the formation of this bond, called an acyl–serine bond, is one product, choline (X), and the enzyme-B intermediate compound (an acetyl–enzyme complex). The water molecule (Y) then reacts with the acyl–serine bond to form the second product, acetic acid (B―Y), which dissociates from the enzyme. Acetylcholinesterase is regenerated and is again able to react with another molecule of acetylcholine. This kind of reaction, involving the formation of an intermediate compound on the enzyme surface, is generally called a double displacement reaction. Sucrose phosphorylase acts in a similar way. The substrate for sucrose phosphorylase is sucrose, or glucosyl-fructose (B―X), and the group N on the enzyme surface is a chemical group called a carboxyl group (COOH). The enzyme-B intermediate, a glucosyl–carboxyl compound, reacts with phosphate (Y) to form glucosyl-phosphate (B―Y). The other product (X) is fructose. In double displacement reactions, the covalent intermediate between enzyme and substrate apparently influences the reaction to proceed more rapidly. Because the enzyme is unaltered at the end of the reaction, it functions as a true catalyst, even though it is temporarily altered during the enzymatic process. Although many enzymes form a covalent intermediate, the mechanism is not essential for catalysis. One substrate (Y) reacts directly with the second substrate (X―B), in a so-called single displacement reaction. The B moiety, which is transformed in the chemical reaction, is involved in only one reaction and does not form a bond with a group on the enzyme surface. The enzyme maltose phosphorylase, for example, directly affects the bonds of the substrates (B―X and X), which, in this case, are maltose (glucosylglucose) and phosphate, to form the products, glucose (X) and glucosylphosphate (B―Y). Covalent intermediates between part of a substrate and an enzyme occur in many enzymatic reactions, and various amino acids—serine, cysteine, lysine, and glutamic acid—are involved. #enzymes #mechanismofenzymeaction #biochemistry #mbbs #medicalstudents #covalentbonds