(e) [S] = 10KM 051000091 ods 26. MATHEMATICAL Determine the values of Kỵ and Vmax for the de- carboxylation of a ß-keto acid given the following data. Substrate Concentration (mol L-¹) 2.500 1.000 0.714 0.526 0.250 Velocity (mM min-¹) 0.588 0.500 0.417 0.370 0.256
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- Assessing the Effect of Active-Site Phosphorylation on Enzyme Activity (Integrates with Chapter 15.) The serine residue of isocitrate dehydroenase that is phosphorylated by protein kinase lies within the active site of the enzyme. This situation contrasts with most other examples of coa1ent modification by protein phosphorylation. where the phosphorylation occurs at a sate remote from the active site. What direct effect do you think such active-site phosphorylation might have on the catalytic activity of isocitrate dehydrogcn.ise? (Sec Barford, D., 1991. Molecular mechanisms for the control of enzymic activity by protein phosphorytation. Biochimica et Biophysica Acta 1133:55—62.)Fozyme Action: An Investigation of Lactase Activity 137 PART F EFFECT OF pH ON ENZYME ACTIVITY Activity of Lactaid at Several pls Observation with Tes Tape" Glucose present? Lactose 90 change More Grean tello Green Hellow NO change Green NO pH 7 Yes, 100 mgloL pH 2 Yes 7100 mglaL pH 10 NO Glucose tes 300 mglaL RART G. EFFECT OF AN INHIBITOR ON ENZYME ACTIVITY Inhibitor Effects Observation with Tes Tape Glucose present? Light Green Teal Yellow IGreen Dark Brown Lactose Yes Lactaid" NO Ethanol Yes Yes Glucose 1. What is the optimum pH of the lactose-conversion reaction, as shown by your data? 2 Did ethanol act as an efficient inhibitor of the lactose conversion to glucose and galactose? 3. Summarize your findings about the concentration, temperature, and pH sensititivity of lactase.. Recall your study of equilibria and kinetics from general chemistry. You used equations with upper case Kand lower case k during the study of equilibria and kinetics respectively. What do the upper and lower case letters refer to?
- not true about the Michaelis-Menten equation? The equation that gives the rate, v, of an the substrate concentration [S] is the Michaelis-Menten equation = Vmax[S]/(Km + [S]), where V, enzyme-catalyzed reaction for all values of max and Km are constants. Which of the following is a) for [S] << Km, V = Vmax applies to most enzymes, but allosteric enzymes have different kinetics when [S] = Km, then v = Vmax/2 gives the rate when the enzyme concentration, temperature, pH, and ionic strength are constant for very high values of [S], v approaches Vmax e) Which is correct about the constant Km in the Michaelis-Menten equation? also called the catalytic constant or turnover number equal to the number of product molecules produced per unit time when the enzyme is saturated with substrate it is the constant in the first order rate equation v = k[A] it is the constant in the second order rate equation v = equal to the substrate concentration at which the velocity or rate of a reaction is ½ the…O BIOCHEMISTRY Understanding major biochemical energy storage and release. A certain anabolic biochemical reaction A has AG- 17.8 kJ mol , and is always coupled to another reaction B, which has two reactants and two products, I this: R + R2 P + P2 The molecule in the drawing area below is either R, or P. • If it's R, change it into P. But if it's P, change it into R. • In either case, draw the molecule as it would exist at physiological pH. • Also please answer the questions about Reaction B in the table below. OR, Was the molecule in the drawing area R, or P, before you changed it? What is R? Enter its common name, usual symbol, or chemical formula: What is P2? Enter its common name, usual symbol, or chemical formula: O BIOCHEMISTRY Understanding major biochemical energy storage and release.. ODO its common name, usual symbol, or chemical formula: NH, -CH N. H OH OH ...... to IIIAn enzyme-catalyzes the isomerization of substrate S to product P. The enzyme has a molecular weight of 120,000 g/mol. In assays using 1 μg of enzyme per assay the Km was 3 x 10^-3M and the Vmax was 2.75 μmole per minute. What would be the Kcat (turnover number or molecular activity) of the enzyme under these conditions? 2.75 min^-1? 3,300,000 min^-1? 330,000 s^-1? 19,800,000 min^-1? 5,500 s^-1?
- The last stop. The final electron acceptor for the electron-transport chain is which of the following? do a. 0202 b. Coenzyme Q с. СО2СО, d. NAD+NAD+Understanding the Mechanisms of Reactions Related to Transketolase The mechanistic chemistry of the acetolactate synthase and phosphoketolase reactions (shown here) is similar to that of the transketolase reaction (Figure 22.30). Write suitable mechanisms for these reactions.Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.
- Regulation of Glutamine Synthetase by Covalent Modification Suppose at certain specific metabolite concentrations in vivo the cyclic cascade regulating E. coli glutamine synthetase has reached a dynamic equilibrium where the average state of GS adenylylation is poised atn=6. Predict what change in nwill occur if: [ ATP ] increases, PIIA/PIID increases, [ -KG ]/[ Gln ] increases, [ Pi ] decreases.Modeling the Regulation of AcetyI-CoA Carboxylase Based on the information presented in the text and in Figures 24.4 and 24.5, suggest a model for the regulation of acetyl-CoA carboxylase. Consider the possible roles of subunit interactions, phosphorylation, and conformation changes in your model.Tracing the Fate of CO2 During Photosynthesis 14C-labeled carbon dioxide is administered to a green plant, and shortly thereafter the following compounds are isolated from the plant: 3-phosphoglycerate, glucose, erythrose-4-phosphate, sedoheptulose-1 .7-bisphosphate, and ribose-5-phosphate. In which carbon atoms will radioactivity be found?