MATHEMATICAL For the following aspartase reaction (see Ques- tion 28) in the presence of the inhibitor hydroxymethylaspar- tate, determine K and whether the inhibition is competitive or noncompetitive. [S] (molarity) 2 1×1 V, No Inhibitor (arbitrary units) V, Inhibitor Present (same arbitrary units) 1010 0010 0.040 0.086 0.120 0.142 × 10-11 01 0.026 5 × 10-4 0.092 1.5 X 10-3 2.5 X 10-3 5 × 10-3 0.150 9. 0.165 S mys
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- MATHEMATICAL For an enzyme that displays MichaelisMenten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? (a) [S]=KM (b) [S]=0.5KM (c) [S]=0.1KM (d) [S]=2KM (e) [S]=10KMMATHEMATICAL If a reaction can be written AB, and the G is 20kJmol1, what would the substrate/product ratio have to be for the reaction to be thermodynamically favorable?REFLECT AND APPLY When we compare the binding of I and of S to the enzyme in a mixed noncompetitive inhibitor, we assumed that the binding of I decreased the affinity of the enzyme for S. What would happen if the opposite were true?
- MATHEMATICAL Determine the values of KM and Vmax for the decarboxylation of a -keto acid given the following data. substrateconcentration(molL1)Velocity(mMmin1)2.5001.0000.7140.5260.2500.5880.5000.4170.3700.256REFLECT AND APPLY In metabolism, glucose-6-phosphate (G6P) can be used for glycogen synthesis or for glycolysis, among other fates. What does it cost, in terms of ATP equivalents, to store G6P as glycogen, rather than to use it for energy in glycolysis? Hint: The branched structure of glycogen leads to 90% of glucose residues being released as glucose-1-phosphate and 10% as glucose.MATHEMATICAL For the Vmax obtained in Question 26, calculate the turnover number (catalytic rate constant) assuming that 131024mol of enzyme were used.
- REFLECT AND APPLY Two biochemistry students are about to use mitochondria isolated from rat liver for an experiment on oxidative phosphorylation. The directions for the experiment specify addition of purified cytochrome c from any source to the reaction mixture. Why is the added cytochrome c needed? Why does the source not have to be the same as that of the mitochondria?MATHEMATICAL The standard free-energy change for the reaction Arginine+ATPPhosphoarginine+ADP is +1.7kJmol1. From this information and that in Table 15.1, calculate the G for the reaction Phosphoarginine+H2OArginine+PiREFLECT AND APPLY Noncompetitive inhibition is a limiting case in which the effect of binding inhibitor has no effect on the affinity for the substrate and vice versa. Suggest what a LineweaverBurk plot would look like for an inhibitor that had a reaction scheme similar to that on page 159 (noncompetitive inhibition reaction), but where binding inhibitor lowered the affinity of EI for the substrate.
- REFLECT AND APPLY 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?REFLECT AND APPLY Would you expect an irreversible inhibitor of an enzyme to be bound by covalent or by non-covalent interactions? Why?REFLECT AND APPLY The malate-aspartate shuttle yields about 2.5 moles of ATP for each mole of cytosolic NADH. Why does nature use the glycerol-phosphate shuttle, which yields only about 1.5 moles of ATP?