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- Describe the structuraldifferences betweenthe oxidized form andthe reduced form ofnicotinamideA biochemical reaction transfers 60 kJ mol-1(15 kcal mol-1) of energy. What general process most likely wouldbe involved in this transfer? What cofactor (or cosubstrate) likelywould be used? Which cofactor probably would not be used?Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)
- At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?What are the three key mechanisms and their associated features that are utilized by enzymes to catalyze reactions. Additionally, which two mechanims of the three you listed does the enzyme chymotrypsin use?When you hold a weight at arm's length, you are not doing any thermodynamic work but the muscles supporting the weight are nevertheless consuming energy. Describe, on the molecular level, how muscles might maintain such state of constant tension without contracting. Why does this state consume ATP?
- Calculate the actual, physiological ΔG for the reaction at 37 °C, as it occurs in the cytosol of neurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6 mM.Assume you have an enzyme that catalyzes a reaction that breaks down dopachrome. At t = 0 s, the absorbance at 475 nm is 0.2 when you add the enzyme. At t = 30 s, would you expect the absorbance to be less than or greater than 0.2?Would you expect an “enzyme” designed to bind to its target substrate astightly as it binds the reaction transition state to show a rate enhancementover the uncatalyzed reaction? In other words, would such a protein actuallybe a catalyst? Explain why or why not.
- When a mixture of 3-phosphoglycerate and 2-phosphoglycerate is incubated at 25°C in the presence of the enzyme phosphoglycerate mutase (which catalyzes the intervconversion of the two substances) until equilibrium is reached, the final mixture contains 6 times as much 2-phosphoglycerate as 3-phosphoglycerate. Which of the following statements is most nearly correct when applied to the reaction shown below: 3-phosphoglycerate ------> 2-phosphoglycerate (R=8.315 J/mole.K) A. △G°' = +12.7 kJ/mole B. △G°' = 0 C. △G°' is incalculably large and positive D. △G°' = -4.44 kJ/mole E. △G°' cannot be calculated from the information gvenAn enzyme contains an active site aspartic acid with a pKa = 5.0, whichacts as a general acid catalyst. On the accompanying template, draw thecurve of enzyme activity (reaction rate) versus pH for the enzyme (assumethat the protein is stably folded between pH 2–12 and that the active siteAsp is the only ionizable residue involved in catalysis). Briefly explain theshape of your curve.Margarine is made from vegetable oil by a chem-ical process. Do you suppose this process converts satu-rated fatty acids to unsaturated ones, or vice versa? Explainyour answer.