Respuesta :
1. Like the concept of a jigsaw puzzle, the competitive inhibitor has a similar structure with the substrate that they can match each other.
2. The noncompetitive inhibitor attaches itself away from the active site of the enzyme.
3. The irreversible/permanent inhibitor forms a covalent bond with an amino acid side group within the active site to prevent the substrate from entering the active site or prevent catalytic activity.
4. Active Site is the site where the competitive inhibitor attaches itself to the enzyme.
5. It is true that the noncompetitive inhibitor binds to the enzyme and causes the distortion of the shape.
6. The interaction between an enzyme and its substrate is disrupted by enzyme inhibitors.
2. The noncompetitive inhibitor attaches itself away from the active site of the enzyme.
3. The irreversible/permanent inhibitor forms a covalent bond with an amino acid side group within the active site to prevent the substrate from entering the active site or prevent catalytic activity.
4. Active Site is the site where the competitive inhibitor attaches itself to the enzyme.
5. It is true that the noncompetitive inhibitor binds to the enzyme and causes the distortion of the shape.
6. The interaction between an enzyme and its substrate is disrupted by enzyme inhibitors.
Answer:
1. A competitive inhibitor exhibits a composition, which is identical to the substrate that can combine with the enzyme just like the substrate.
2. A noncompetitive inhibitor combines with the enzyme that is not the active site.
3. Generally, a irreversible inhibitor produces a covalent bond with an amino acid group within the active site that inhibits the substrate from entering the active site or inhibits catalytic activity.
4. The competitive inhibitor competes with the substrate for the active site present on the enzyme.
5. When the noncompetitive inhibitor gets combined with an enzyme, the shape of the enzyme gets distorted.
6. The enzyme inhibitors disrupts the usual associations between an enzyme and its substrate.