Please explain question 26 ing a solution con-ity. Why is the de-solution containsplain the reactiond rate data fit theFindings prove thealyst alter the stan-have on the acti-33AD3# 8Formation of ATPct on the rate ofalyst increase theW JIADSA CAA? With respectuggest how manyed in the detaileddrogenase cata-_D+aviolet region ofnot. Suggest anthis reaction, as-nmeter capable ofeter to monitorestion 14? Whyng out enzymaticinduced-fit mod-the lock-and-key6-4 The Michaelis-Menten Approach toEnzyme Kinetics22. RECALL Show graphically how the reaction velocity dependson the enzyme concentration. Can a reaction be saturated withenzyme?23. RECALL Define steady state, and comment on the relevance of thisconcept to theories of enzyme reactivity.24. RECALL How is the turnover number of an enzyme related toVmax?25. MATHEMATICAL For an enzyme that displays Michaelis-Mentenkinetics, what is the reaction velocity, V (as a percentage of Vmax),observed at the following values?(a) [S] = KM(b) [S] = 0.5 KMgain (c) [S] = 0.1 KM(d) [S] = 2KMKrautReview Exercises(e) [S] = 10KM26. MATHEMATICAL Determine the values of Kỵ and Vmax for the de-carboxylation of a B-keto acid given the following data.srisSubstrate Concentration (mol L-¹)2.5001.0000.7140.5260.250165Carbon Dioxide Concentration(mmol L ¹)27. MATHEMATICAL The kinetic data in the following table were ob-tained for the reaction of carbon dioxide and water to producebicarbonate and hydrogen ion catalyzed by carbonic anhydrase:CO, + H,O → HCOỹ +H*1.252.55.020.0Velocity (mM min-¹)0.5880.5000.4170.3700.256[H. De Voe and G. B. Kistiakowsky, J. Am. Chem. Soc. 83, 274 (1961)].From these data, determine KM and Vmax for the reaction.1/Velocity(M¹ sec)36 × 10³20 × 10³12 × 10³6 × 10³28. MATHEMATICAL The enzyme B-methylaspartase catalyzes the

Km and Vmax are kinetic constants that help to determine the efficiency of an enzyme.Km is equal to…

Answered: (e) [S] = 10KM 051000091 ods 26.…

Biochemistry

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Chapter18: Glycolysis

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. 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?
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.
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 III
An 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+
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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.
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(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