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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- In the rete mirabile serving the red swimming muscles oftunas, some key enzymes of catabolism show gradients ofconcentration: They are more concentrated at the cold end of therete, and less concentrated at the warm end. These variationsparallel variations that are often seen in the thermal acclimationof poikilotherms, when enzyme concentrations rise duringacclimation to cold and fall during acclimation to heat. Whatdo you think could be some of the reasons for these spatial andtemporal variations in enzyme concentration? Why not havethe highest observed enzyme concentrations everywhere at alltimes?Allosteric regulation O The product of a series of reactions acts as an inhibitor for an earlier reaction. O Hormones control the synthesis of enzymes. A regulator binds to the enzyme at a site other than the active site. This binding changes the shape of the enzyme and alters the catalytic ability of the enzyme. An inhibitor binds reversibly to the enzymesubstrate complex, blocking the binding of the second substrate to the active site. The activity of an enzyme is influenced by the addition or removal of a group that is covalently bonded to the enzyme. O An inhibitor forms covalent bonds to the active site. permanently blocking it.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.
- Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout,several medications are used to inhibit the activity of xanthine oxidase and reduce theproduction of uric acid. You are a biochemist and just discovered a chemical that can inhibitthe activity of the human xanthine oxidase. When analyzing its mode of inhibition, you foundthat the enzyme inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displayskinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministryof health for approval as a medication for gout. Based on the data provided, are they going toauthorize it as a medication or not? Explain?(notice that its 450 kj not 450j)Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout,several medications are used to inhibit the activity of xanthine oxidase and reduce theproduction of uric acid. You are a biochemist and just discovered a chemical that can inhibitthe activity of the human xanthine oxidase. When analyzing its mode of inhibition, you foundthat the enzyme inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displayskinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministryof health for approval as a medication for gout. Based on the data provided, are they going toauthorize it as a medication or not? Explain? Please be aware that energy is 450 kJ.mol-1, not 450 J.mol-1Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout,several medications are used to inhibit the activity of xanthine oxidase and reduce theproduction of uric acid. You are a biochemist and just discovered a chemical that can inhibitthe activity of the human xanthine oxidase. When analyzing its mode of inhibition, you foundthat the enzyme inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displayskinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministryof health for approval as a medication for gout. Based on the data provided, are they going toauthorize it as a medication or not? Explain? (notice that its 450 kj not j)
- 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.In bacteria, isocitrate dehydrogenase is regulated by phosphorylation of a specific Ser residue in the enzyme active site. X-ray structures of the phosphorylated and the nonphosphorylated enzyme show no significant conformational differences. How does phosphorylation regulate isocitrate dehydrogenase activity? O The phosphoryl group sterically hinders the substrate. O The phosphorylation bears a negative charge, which repels the substrate. O The phosphoryl group attracts positively charged Ca2* cations, which block the active site on the enzyme. None of the above.WMapp E+S ES E+P Vmax Km =Vmax 2 -1 a = 1+ [1]/K, X intercept = Kcat [E]T Km Question 6 In the simple enzyme-catalyzed reaction below, which of the rate constants would be second-order? E+S ES →E+P k-1 O k2 O k-1 O k1
- 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?If you graph the velocity of an enzymecatalyzed reaction vs. [S] for each of two substrates that are partof a random mechanism, would you expect to see the same shapecurve? Why or why not?How Is Metabolism Regulated? (Integrates with Chapter 15.) Metabolic regulation is achieved via regulating enzyme activity in three prominent ways: allosteric regulation, covalent modification, and enzyme synthesis and degradation. Which of the.se three modes of regulation is likely to be the quickest; which the .slowest? For each of these general enzyme regulatory mechanisms, cite conditions in which cells might employ that mode in preference to either of the other two.