Explain why burst kinetics are observed for one chromogenic substrate but not another.
Chromogenic substrate are synthetically made and are designed to be highly selective as the natural substrate for that particular enzyme. And it follows single substrate mechanism in which that enzyme binds only one substrate. We know that, burst kinetics is a form of enzyme kinetics therefore burst kinetics are observed for one chromogenic substrate but not another due to chromogenic substrate's highly selective nature.
Explain why burst kinetics are observed for one chromogenic substrate but not another.
What kind of kinetics is observed in an enzymatic reaction, under conditions where the substrate concentration is much higher with respect to KM ([S] >> KM)? Assume that a monomeric and non-allosteric enzyme is considered. A. Cooperative B. First Order C. Zero Order D. The systerm is at equilibrium and no reaction occures E. Second Order
Why might we make enzymes that work on the same substrate, but with different enzyme kinetics? How do the different hexokinase isozymes of liver and muscle reflect the different roles of these organs in carbohydrate metabolism? Why is the fact how hexokinase 4 is not inhibited by glucose 6-phosphate, instead being inhibited by reversible binding of a regulatory protein specific to liver be important in its function?
What is a burst phase? (Drawing a graph here would be helpful). Explain how the detection of a burst-phase in the short-timescale kinetics of the chymotrypsin enzymatic reaction helped researchers elucidate the mechanism of this enzyme reaction cycle?
In 50 words or more explain how chemical kinetics and chemical equilibrium are related to one another. Give a real world example of chemical kinetics.
Answer the following questions related to burst time prediction. A. Discuss why it is important to know the length of the next job or CPU burst and which scheduling algorithm requires future knowledge. B. Estimate the burst times under the following conditions: Tau = 12 Alpha=.25 Actual observed burst times are: 10, 15, 13, 10 C. Estimate the burst times under the following conditions: Tau = 12 Alpha=.75 Actual observed burst times are: 10, 15, 13, 10 D. What is...
. 52. What is a burst phase? (Drawing a graph here would be helpful). Explain how the detection of a burst-phase in the short-timescale kinetics of the chymotrypsin enzymatic reaction helped researchers elucidate the mechanism of this enzyme reaction cycle? 51. Draw a michaelis-menten graph (at right) and a linweaver burke (double-reciprocal) plot (at left) of an uninhibited enzymatic reaction. Be sure to label the axes with appropriate labels. In each of these TWO graphs, using the uninhibited curves as...
If the substrate concentration is varied with a fixed concentration of enzyme, it is observed that at low substrate concentrations that overall order while at high substrate concentrations, the reaction will be overall order. Select one: a. first; second b. first; third order c. first; zero d. second; second e. second; pseudo first order
b. Look at the graph below of how a competitive inhibitor affects the kinetics of an enzyme C. Rate of reaction is the Vmax of the enzyme affected? Why or why not: explain in terms of substrate concentration and enzyme active site saturation) Without inhibitor With competitive inhibitor d. is Vmax/2 affected? Why or why not: explain in terms of Vmax. Substrate concentration e. Is Km affected? Explain in terms of the active site. Hint a competitive inhibitor is competing...
Kinetics Question: a) Explain why the rate of reaction must be defined in a manner that is not dependent on which reactant or product is used to measure it. b) Explain why rate laws must be determined experimentally. c) Explain how the rate limiting step in a mechanism determines the overall reaction rate.
24. Explain the energetic benefits of making the enzyme active state rather than to the substrate conformation. Also explain how contribute to enzyme action. In other words, how do these weak intera enzyme and the transition state lower the activation energy?) of making the enzyme active site complementary to the transition nation. Also explain how multiple weak interactions words, how do these weak interactions between the 25. 1/F. The pk's of titratable groups of amino acids remain constant irrespective of...