Compare and contrast the activity of enzyme inhibitors and co-enzymes and their function in regulating enzymes.
1. Coenzymes are organic compounds, which are generally non-protein in nature. They bind to the enzyme and helps it catalyse a reaction. Whereas enzyme inhibitors are molecules, that binds to the enzyme, and decreases or inhibits its biological activity.
2. Most enzymes require coenzymes for functioning. When a coenzyme binds to the active site of an apoenzyme (enzyme devoid of coenzyme), then a holoenzyme is formed. This holoenzyme can efficiently catalyse a reaction. All enzymes work efficiently if they are not inhibited by enzyme inhibitor molecules by binding to the active site of the enzyme and inhibiting the substrate from binding to the active site.
3. Enzyme inhibitors can be irreversible inhibitors and reversible inhibitors. No such classes are found in case of coenzymes.
4. Examples - Coenzyme : Vitamin
Reversible inhibitor : Protease inhibitors
Irreversible inhibitor : Diisopropylfluorophosphate
Compare and contrast the activity of enzyme inhibitors and co-enzymes and their function in regulating enzymes.
Compare and contrast the general structure and function of active sites for two different enzymes—one which digests fats, and one which digests polysaccharides
What are the advantages to regulating enzyme activity through phosphorylation? How does it differ from allosteric regulation and how is it similar? Are there any advantages to phosphorylation versus allosteric regulation of protein function?
Feedback inhibition is defined as a mechanism of down-regulating enzyme activity by the accumulation of a product earlier in the pathway. True or False, please explain
Enzyme inhibitors are used in the treatment of many diseases. Among the targets for pharmaceutical intervention are the HIV proteases E.C.3.4.13.16. Look online for enzyme databases and sources of drug information that describe the structure and function of either one of these viral enzymes. What inhibitor(s) are known for your enzyme? Is the inhibitor competitive or noncompetitive?
15. Compare the catalytic activity of of the following enzymes: carbonic anhydrase, aspartate transcarbomylase (ATcase), restriction enzymes and myosins. (40 points) What is unique about each active site with regards to types of amino acid residues a) located in active site and interaction with substrate? b) Briefly what is the mechanism of catalysis in each active site? Are cofactors or coenzymes required by the enzymes and if so what is the role of the cofactor/coenzyme in catalysis? c) How is...
Inhibitors of enzymes have no effect on kinetic constants O All statements O do not directly interact with enzymes O can decrease rates of enzyme-catalyzed reactions
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menton plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. see for instance: http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 1 µM and a different variant has a Km of 10 µM....
Enzymes 1. Briefly describe three factors that could alter the activity of an enzyme. 2. How do you think the optimal temperature for enzymes found in thermophile bacteria living in hot pools differ from that of the enzymes found in your body? 3. How do you think the optimal pH of enzymes in the stomach compares to the optimal pH for enzymes in blood? 4. Take a look around your house and identify household products that work by means of...
Enzymes Temperature is an important factor that can regulate enzyme-mediated functions. Temperature is one of the tightly homeostatically controlled variables in the human body. What are the symptoms of loss of temperature control during a high fever? Explain why these symptoms occur based on enzyme function and cell signaling effects that are dependent on temperature. Based on Figure 1, explain how the temperature optimum of the activity of enzymes is expected to differ in organisms depending on where they live....
Metabolism can be regulated via Group of answer choices regulating synthesis of particular enzyme. allosteric effectors. feedback inhibition. covalent modification of enzymes. All of the above.