Describe the enzyme carbonic anhydrase by answering the following question:
(a) Which reaction is catalyzed by this enzyme? (2 points)
(b) Which cofactor is used by this enzyme? (1 point).
(c) Which amino acids of the enzyme, and how many of them coordinate the cofactor? (2 points).
(d) How does this cofactor help accelerate the reaction? Think about the chemistry (1 point) and the shift of the equilibrium (1 point).
(a) it helps in converting the CO2 and water to form carbonic acid which further disassociates into bicarbonate ions. it increases the speed of reaction.
(b) Zn+2 ion works as a cofactor for this enzyme.
(c) Histidine amino acids of enzymes coordinate with the cofactor zinc.
(d) the water molecule binds with positively charged Zn ions which reduce the Pka of water from 15 to 7 . zinc-bound hydroxide ion is sufficiently nucleophilic to attack CO2 much more readily than water does.
Describe the enzyme carbonic anhydrase by answering the following question: (a) Which reaction is catalyzed by...
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...
Which reactions is catalyzed by carbonic anhydrase in the red blood cell when it reaches the lung? 1. H+ +HCO3->H2CO3 2. H2CO3 ---->H+ + HCO3- 3. H2CO3->CO2+H20 4. CO2 + H20 -> H2CO3
The enzyme carbonic anhydrase catalyzes the reaction CO2(g)+H2O(l)−→−HCO3−(aq)+H+(aq).CO2(g)+H2O(l)→ HCO3−(aq)+H+(aq). In water, without the enzyme, the reaction proceeds with a rate constant of 0.039s−10.039 s−1 at 25°C.25 °C. In the presence of the enzyme in water, the reaction proceeds with a rate constant of 1.0×106s−11.0×106 s−1 at 25°C.25 °C. Assuming the collision factor is the same for both situations, calculate the difference in activation energies for the uncatalyzed versus enzyme- catalyzed reaction.
Need help with number 13! I already asked about number 12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
A biochemist was exploring the properties of Enzyme X . Enzyme X catalyzed the following reaction. Galactose-3-phosphate <---> Galactose-2-phosphate. How might the biochemist show that the reaction reaches equilibrium? How would the biochemist calculate the equilibrium constant?
Which one change would be most likely to decrease the deltaG of an enzyme-catalyzed reaction, according to our coverage? Use a version of the enzyme with a lower Kcat. Use a version of the enzyme with a lower Km. Find a way to remove product of the reaction (eg, by consuming that product in another reaction) Add a noncompetitive inhibitor. Double the enzyme concentration QUESTION 14 Think about an 800-amino acid polypeptide. In the middle (let's say amino acids 401-402)...
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....
2-In an enzyme-catalyzed reaction, the rate of the reaction depends on which of the following at very low substrate concentrations? Select one: Neither enzyme concentration nor substrate concentration Enzyme concentration but not substrate concentration Substrate concentration but not enzyme concentration Both substrate concentration and enzyme concentration
Question 2 2.5 pts Which of the following statements is (are) true about enzyme-catalyzed reactions? The reaction is faster than the same reaction in the absence of the enzyme. The free energy change of the reaction is opposite from the reaction in the absence of the enzyme. The reaction always goes in the direction toward chemical equilibrium. O A and B only. O A, B, and C.
Help with 22, 25, 26, 27, 28, 29 please and any others as well 22. Draw the structure of glycine. Draw the structure of valine. Now draw them as a dipeptide. 23. Complete the following dehydration synthesis reaction: Glycine + Valine - Dipeptide + 24. What 2 functional groups are found in every amino acid? 25. All amino acids have a chiral carbon except glycine. Why? 26. If you pour H2O2 (hydrogen peroxide) on a cut or skin scrape, it...