The answers are as follows:
1. <span>An inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate: t</span>his is called competitive inhibitor. A competitive inhibitor will compete with the substrate for the active site of the enzyme and bind to the active site, thus incapacitating the substrate from binding to the active site.
2. An inhibitor binds to a site on the enzyme that is not the active site: this is called non competitive inhibitors. Non competitive inhibitors bind to other site in the enzyme which is not the active site of the enzyme. The binding of the inhibitor changes the conformation of the enzyme as well as the active site, thus making it impossible for the substrate to bind to the enzyme effectively.
3. <span>usually, a(n) inhibitor forms a covalent bond with an amino acid side group within the active site, which prevents the substrate from entering the active site or prevents catalytic activity: this is called irreversible or permanent inhibition. Permanent inhibitors form covalent bonds with the enzyme and prevent substrate from binding to the enzyme.
4. T</span><span>he competitive inhibitor competes with the substrate for the ACTIVE SITE on the enzyme: The active site of an enzyme is the place where the substrate normally bind in order to activate a enzyme. Competitive inhibitors are those inhibitors that compete with the substrate for the active site of the enzyme and prevent the substrate from binding there.
5. W</span><span>hen the noncompetitive inhibitor is bonded to the enzyme, the shape of the ENZYME is distorted. The non competitive inhibitors are those inhibitors that bind to other places in the enzyme instead of the active site. The binding of the non competitive inhibitor usually distort the shape and the conformation of the enzyme thus preventing the substrate from binding to it effectively.
6. E</span><span>nzyme inhibitors disrupt normal interactions between an enzyme and its SUBSTRATE. The principal function of enzyme inhibitor is to prevent the substrate from binding to the appropriate enzyme. This is usually done in the human system in order to regulate the activities of enzymes.</span>
the universe consists of all existing matter, energy, and space.
Answer:
Methemoglobinemia
Explanation:
Methemoglobinemia (also known as the blue baby syndrome), is a condition with multiple etiologies which is associated with the lack of oxygen in the blood. This syndrome affects the function of red blood cells by altering the amount of hemoglobin protein, which carries and distributes oxygen to the body. Methemoglobinemia may be acquired by exposure to drugs and/or toxins. In this regard, it has been shown that high levels of nitrates in the water may induce this syndrome in infants.
A major study has shed new light on the dim layer of the ocean called the "twilight zone" -- where mysterious processes affect the ocean's ability to absorb and store carbon dioxide accumulating in our atmosphere.
Answer: The answer is that the phenotypic ratio among phenotypes produced from an F1 X F1 dihybrid cross is 9:3:3:1.
Explanation:
Independent assortment of genes explains how alleles on different chromosomes arrange independently of one another during gamete formation.
So, a dihybrid cross involving TWO characters (e.g Seed color & seed shape) would have its respective alleles DISTRIBUTED whether dominant or recessive, for crossing to occur and yield varying proportion of offspring in the well spread ratio of 9:3:3:1; making it a consequence of independent assortment of genes
