4. Enzyme performance (a) Compare chymotrypsin, MutY, and carbonic anhydrase interms of chemical difficulty. (Hint: compare kcat). (b) Which enzyme is faster? And byhow much? (c) Draw a molecular sketch comparing TS stabilization strategies for Mutyand chymotrypsin. (d) Compare chymotrypsin, Muty, and carbonic anhydrase in termsof how quickly they find their substrates. (Hint: compare kcat/KM). Which enzyme hasthe more "perfect" enzyme performance rating? (e) What is the molecular explanation forthe apparently impossible fast rate at which Muty finds its substrate? (f) What is thebiological constraint demanding this very high level of enzyme performance?Enzyme\ParameterCarbonic anhydraseMutyChymotrypsinkcat (s-1)600,0000.2100KM (M)0.0081.2 x 10-100.005

Turnover number (kcat) is the maximum number of substrate molecules that can be converted into…

Answered: Enzyme performance (a) Compare…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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24. Researcher X did a series of experiments and determined the following about Enzyme A and its substrate (S). KM - 4 mM Vmax 100 mM/s axis. (. a) Draw the Michealis-Menton plot with all the above information shown. Be sure to label Vmax Rate of neation (mm) rate of react in mm. supstratiate concentration MM/S b) Convert the Michealis-Menton plot into a Lineweaver-Burk plot below, Label the axis. Vmax Rate of reaction (MM) 8 100 90 Go 100 80 - tmax 30 201 c) Using a dotted line, add in how á uncompetitive inhibitor how the rate would look with (S) (MM/S) x 1|S an uncompetitive inhibitor added. 100 KOMI Ke Vmax Vmar Sun competiti 6 • substante (MMIS)
4.Pepsin is the proteolytic enzyme of gastric juice. The active form of this enzyme is formed from pepsinogen under HCL action.Optimum of enzyme action: pH = 1.5, t = 37°. Describe the properties of this enzyme. For this:1)Name and explain the mechanism of this enzyme activation.2)Draw the plot and explain the effects of pH and t on the reaction velocity.3) Explain how changes the velocity of this reaction in patients suffering from hypoacidie gastritis.
1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:
5.5 Explain the effect of each type of inhibitor on the apparent kinetic parameters: (1) Inhibitor binds only free enzyme does Km increase, decrease, not change? does Vmax increase, decrease, not change? (2) Inhibitor binds only ES complex does Km increase, decrease, not change? does Vmax increase, decrease, not change? (3)Inhibitor binds E and ES equally does Km increase, decrease, not change? does Vmax increase, decrease, not change?
2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…
III. Protein: QQICIMFELTQISS Predict the products of the following reactions with the protein given, if there is none, write NO RXN. Also indicate, if the reaction is fast or slow. 9.) КОНРЫ(СH-CО)» 10.) Glyoxilic Acid/Conc. H2SO4
3) Consider the oxidation of an organic acid: C18H3602(s) + 2602(g) → 18CO2(g) + 18H20 (1) a) Compute the RER. b) b) Determine the rate of energy expenditure at rest (RMR) if the rate of oxygen consumption 1.25 is liter/minute. c) How much energy will be burned if the exercise will proceed for 1 hour?
1. For enzyme catalyzed reaction: ki S + E=X (fast) k2 X -2> P + E (slow) derive the rate law and answer the following: a) What is meant by Michaelis-Menten constant km? (b) Prove that order of reaction in substrate changes from unity to zero at higher [S]. (c) What is the rate and value of km, if k2 >> k1. (d) Draw the potential energy diagram for enzyme catalyzed reaction.
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16. The overall reaction for the glycolysis reaction is C6H₁2O6(aq) + 2NAD+ (aq) + 2ADP³(aq) + 2HPO(aq) + 2H₂O(1) 2CH3COCO₂ (aq) + 2NADH(aq) + 2ATP4 (aq) + 2H3O+ (aq). What is A,G at chemical equilibrium?
1.In a kinetics data set, in case a substrate concentration is given [S] in uM and inhibitor concentration [I] uM, initial velocity (Vo) in umol/min , Km , Vmax, apparent Km, apparent Vmax, and Ki, is there any way of finding Kcat ? 2.Which formula would be used in that case? What would the process be for finding Kcat?

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