Concept explainers
(a)
Interpretation:
The values of
Concept introduction:
If the concentration of enzyme is constant and the substrate concentration is gradually increased, the reaction velocity also increases up to a maximum and after that it will remain constant even though the substrate concentration increases further.
The Michael is constant, KM is the substrate concentration at half of the maximum velocity. The smaller the KM of an enzyme, the smaller the amount of substrate required to saturate the enzyme.
kcat refers to the turn over number which is defined as the number of substrate molecules that is converted to product by each enzyme site per unit time.
(b)
Interpretation:
The reason for the occurrence of oxygenation reaction should be determined.
Concept introduction:
The ratio between turn over number and Michael is constant;
Want to see the full answer?
Check out a sample textbook solutionChapter 20 Solutions
BIOCHEMISTRY-ACHIEVE (1 TERM)
- ch Select all statements that are correct. Note there might be more than 1 correct statement. From the Lineweaver-Burk plot the equilibrium constant (Keq) can be obtained The Lineweaver-Burk plot gives a more accurate prediction for Vmax than the Michaelis- Menten plot The Lineweaver-Burk plot assumes that products and reactants are present at equal concentrations during the entire time of the reaction The Lineweaver-Burk plot shows velocity of reaction vs substrate concentration The Lineweaver-Burk plot shows 1/velocity of reaction vs 1/substrate concentration O 20°C D) // Earrow_forwarda. Use the values in Problem 23.31 to calculate the energy change in the following reaction. fructose 1,6-bisphosphate + ADP--------> fructose 6-phosphate + ATP b. Is this reaction energetically favorable or unfavorable? c. Write this reaction using curved arrow symbolism. d. Can this reaction be used to synthesize ATP from ADP? Explain.arrow_forwardConsider docosanoic acid C12H43CO2H a. Label the alpha and beta Carbons. Show the beta-oxidation in an EXPANDED structure. b. Draw each acyl CoA derived from this fatty acid. c. How many acetyl Co A molecules are formed by complete beta-oxidation? d. How many cycles of beta-oxidation are needed for complete oxidation? e. How many molecules of ATP are formed from the complete catabolism of this fatty acid? Show the complete computation. f. How many moles of ATP per gram of fatty acid is formed from the complete catabolism of the given fatty acid? g. What is the molar mass of the given fatty acid? Solution: Show here the complete computations, [from a to e]arrow_forward
- Worksheet on Computation of ATP yield from Fatty acid metabolism. Consider docosanoic acid, C21H43CO2H a. Label alpha (a) and beta ( B) carbons b. Draw the acyl COA derived from this fatty acid c. How many acetyl CoA molecules are formed by complete B-oxidation? d. How many cycles of B- oxidation are needed for complete oxidation? e. How many molecules of ATP are formed from the complex catabolism of this fatty acid.arrow_forwardEnzyme X exhibits maximum activity at pH = 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. a Tyr residue on the enzyme is involved in the reaction. a His residue on the enzyme is involved in the reaction the enzyme uses NADH has a cofactor. the enzyme uses coenzyme A has a cofactor.arrow_forwardOH affromah. The Standard free energy CAGO¹) of the reaction shown above can be estimated based on? OH A. High Energy bands B. Reduction potential C. cannot be estimated OH energy. он The reaction shown above requires the cofactor to proceed forward without significant was te of A.ATP B. Nicotinamide C. Flavin D. No cofactor required 3 Determine approximate 46°1 of the coupled reaction KJ/mol possible answers: (0,-8,-15,-22,-30, -38,-45) The class of enzyme that catalyzes the reaction is possible answers: Mutase, Isomerase, ki nase, phosphatase, Dehydrogenase, Aidolasearrow_forward
- a. Describe in your own words, 5 assumptions that must be made in order to apply a Michaelis-Menten kinetic model to an enzymatic reaction. providing a mathematical expression or inequivalent (">" or "arrow_forwardSuppose that the data below are obtained for an enzyme catalyzed reaction in the presence and absence of inhibitor Y. [S] (mM) V (mmol/mL*min) Without Y With Y 0.2 5.0 2.0 0.4 7.5 3.0 1.8 10.0 4.0 1.0 10.7 4.3 2.0 12.5 5.0 4.0 13.6 5.5 a.) Determine the type of inhibition that has occurred b.) Does inhibitor Y combine with E, with ES or with both? Explain c.) Calculate the inhibitor constant, Ki, for substance Y, assuming that the final concentration of Y in the reaction mixture was 0.3mMarrow_forwardCHOOSE THE CORRECT LETTER 1.Which of the following substrates is used in the first oxidation step of the Kreb's cycle to produce NAH and CO2?A. isocitrateB.a-ketoglutarateC. citrateD. succinyl-CoA 2.What is the reason for isomerization of citrate to isocitrate?A.The reaction converts a tertiary alcohol, which cannot easily be oxidized, to a secondary alcohol that can be oxidizedB. Isocitrate protects cells from the toxic effects of arsenite ion.C. The reaction is one major regulatory step for the citric acid cycle because it functions as a rate limiting step.D. Isocitrate is a substrate for a reaction that occurs spontaneously without enzymatic catalysisarrow_forward
- Please choose the correct letter . and explain a bit why you choose it According to the second law of thermodynamics, a. energy will not be destroyed b. energy will not be created c. potential energy will always increase d. entropy will always increase e. both a and b are correct 2. In one of the reactions of the citric acid cycle, malate is oxidized to oxaloacetate. When this reaction is considered in isolation, a small amount of malate remains and is not oxidized. The best term to explain this is a. enthalpy b. entropy c. equilibrium d. free energy e. loss of energyarrow_forwardDirections: Solve the following problem: The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate: CH,NH, CH OOC-CH-CH-COOOOC-CH-CH-COO+NH mesaconate Williams and Selbin The effects of hydroxymethylaspartate as an inhibitor for this enzyme was studied. The following data wer Substrate Concentration obtained: Reaction Rate without inhibitor (mM) 1 × 10-4 5 x 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 (mM/s) 0.026 0.092 0.136 0.150 0.165 Reaction Rate with inhibitor (mM/s) 0.010 0.040 0.086 0.120 0.142 Use Lineweaver-Burk plot to determine the KM and Vmax of the enzyme in the absence of inhibitor. Moreover, determine as well whether the inhibitor is competitive or noncompetitive. Show the graphs and calculations below.arrow_forwardA. Identify different types of organic reaction mechanims in the following metabolic pathways.4. Conversion of Pyruvate to Acetyl CoA5.Citric acid cycle6. Gluconeogensis pathway (pyruvate to glucose) B. Identify at most 5 organic reactions for each metabolic pathway.arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON