The flux through a metabolic pathway with 10 enzymes increases by 10% which the concentration of enzyme 4 is doubled, increases by 70% when the concentration of enzyme 2 is doubled, but does not change when the concentration of enzyme 7 is doubled. Which enzyme is most likely modulated by a regulatory metabolite or post- translational modification? O All are equally likely to regulated enzyme 4 enzyme 2 enzyme 7
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- When enzyme solutions are heated, there is a progessive loss of catalytic activty over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 degrees Celsius lost 50% of its activity in 12 minutes, but when incubated at 45 degrees Celsius in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates.Many enzymes obey simple Michaelis–Mentenkinetics, which are summarized by the equationrate = Vmax [S]/([S] + Km)where Vmax = maximum velocity, [S] = concentration ofsubstrate, and Km = the Michaelis constant.It is instructive to plug a few values of [S] into theequation to see how rate is affected. What are the rates for[S] equal to zero, equal to Km, and equal to infinite concen-tration?Regarding the physical condition (characteristics of the solution/environment) in which an enzyme finds itself: sometimes enzymes are most active at a certain level and still active but to a lesser degree at a level above or below the optimal level. Describe the likely reason for the enzyme’s decrement in function at levels other than the optimal level?
- All metabolic pathways must be regulated to maintain homeostasis. The catalytic activity of anenzyme can be controlled allosterically and/or by reversible covalent modification. Provide anexample of each type of regulation (allosteric and reversible covalent modification) in the contextof a metabolic pathway. Be specific, and be sure to explain the rationale behind the regulatorystrategy.After the training of marathon, lactic acid is accumulated in the athlete's thigh muscle. Compare the physiological functions and Vmax of glycogen phosphorylase in actively working skeletal muscle and that in liver After vigorous exercise, the athlete faints due to low blood glucose level. A liver biopsy test shows excess amount of glycogen is present in the liver. Suggest with explanation, which type of enzyme is defective in this case.A generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.
- PART IV. HOW FAST DOES IT GO?Another member of your research group studied the kinetics of theGAPDH from the organism. They also determined if the GAPDH fromthe organism is also inhibited by the known inhibitor of GAPDH fromhumans. A. From the following data, determine the KM (Michaelis-Menten Constant) and the Vmax(maximum velocity) of the enzyme without and with the inhibitor. B. If GAPDH is inhibited, what specific type of inhibition is observed?One substrate name is X, and this substrate have two enzymes.(E1and E2) E1and E2, are enzymed and they related in the synthesis of an amino acid and an antibiotic, respectively.Reaction rates of enzymes , at an optional concentration of E1and E2 were determine at different concentrations of substrate X. Which data is suitable labeled for E1 and why ?Another member of your research group studied the kinetics of theGAPDH from the organism. They also determined if the GAPDH fromthe organism is also inhibited by the known inhibitor of GAPDH fromhumans. From the following data, determine the KM (Michaelis-Menten Constant) and the Vmax(maximum velocity) of the enzyme without and with the inhibitor.
- In any given enzyme, the active site is only a small portionof the entire molecule. Synthesis of such a relatively largemolecular machine requires an enormous amount of cellular energy. Explain why this inefficiency is tolerated.A model is proposed to explain the reaction catalyzed by an enzyme. Experimentally obtained rate data fit the model to within experimental error. Do these findings prove the model?6. Reciprocal regulation of opposing pathways is necessary to avoid the wasteful synthesis anddegradation of metabolic intermediates. Provide two distinct examples of reciprocal regulation. Bespecific, and be sure to explain the conditions that signal enzyme activation and/or inhibition.