Question 7 of 16©MatOne way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover numberis the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The tablegives the turnover number of four representative enzymes.WF2#m3EHow many molecules of fumarate can one molecule of fumarase act on in 29.0 min?DfumarateLactate dehydrogenase lactatefumarate molecules:F3>EnzymeRibonucleaseFumarase$4RUreaseFF4%5TGB6HOLOF5Substrate Turnover number (per second)RNA100800100010.000YH&7urcaF6UJDELL*8COF7K(9FBOP;manWiF10[F111F12BackspaceEnterInsertPrintScreenShiftDeleteHomeScrollLockAnswerEnd8:24 PM10/15/2023+PgUpPauseBreakPgDnNumLock7Home41Enc

Kcat, or turnover number is the number of substrate molecules converted to product at one active…

Answered: One way of expressing the rate at which…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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QUESTION 4 What TYPE of inhibition is observed in the following: S E Competitive Non-competitive Uncompetitive Allosteric
QUESTION 1 What TYPE of inhibition is observed in the following plot: V max Vo O O KK Competitive Non-competitive Uncompetitive Allosteric [S], mM
QUESTION 10 Select a property that does not belong to allosteric enzymes. They conform to hyperbolic Michaelis-Menten kinetics They may have binding sites for regulatory molecules that are separate from active sites They tend to have a signmoidal curve of rate versus [S] They undergo conformation changes as a result of modulator binding.
QUESTION 2 What TYPE of inhibition is observed in the following plot: 1/v₂ Intersect at Y axis 1/Km Competitive Non-competitive Uncompetitive Allosteric 1/V, max 1/[S]
Question 2 of 13 Fill in the blanks: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, Mif both statements are incorrect. A. The dissociation of the ES complex to the product is more energetically favored than its dissociation into the separate enzyme and substrate. B. The rate determining step in enzymatic catalysis is the binding of the substrate to the active site of the enzyme.
QUESTION 3 Biocatalysts are effective because: O a. They increase the activation energy of a reaction Ob. They stabilize the transition state O. They decrease the rate of the reaction Od. They decrease the activation energy of a reaction QUESTION 4 Which of the following statements is INCORRECT regarding L-amino acids and D-amino acids? O NH3 group on the left of the chiral carbon in both isomers O b. They are nonsuperimposable mirror images of each other O NH group on the left of chiral carbon in L isomers Od. They are enantiomers
Question 2. Answer the following questions: A. The following experimental data was collected during a study of the catalytic activity of anintestinal peptidase with the substrate glycylglycine. Plot the data as a graph, and use it toestimate the Km and the Vmax for this enzyme. B. Now transform this data to plot it as a straight line (Lineweaver-Burk plot). Determine Km andthe Vmax for this enzyme using this new plot. Do your results agree with the estimates made fromthe first graph of the raw data (from 2A)? C. Now assume that the activity of this intestinal peptidase is regulated by covalent modificationof its catalytically active amino acid. Upon phosphorylation, the Km of the catalyzed reaction has been observed to increase by a factor of 3 without any effect on its Vmax. Is the enzyme getting activated or inhibited upon phosphorylation? Justify your answer. D. How will the Lineweaver-Burk plot of the phosphorylated enzyme differ from the plot of the unmodified enzyme (from 2B)?…
Question 6 of 19 Proteasomal proteases can be inhibited by compounds such as ixazomib (shown below). How does this compound inhibit protease activity? HO Ixazomib O Uncomptetitively O Competitively O Noncompetitively
Time 3/33 answered Ở Show Hewtty, Carlos Remaining Please save all answers. Questions that you save can still be edi pu have 1 UNSAVED ANSWER- SAVE ALL ANSWERS Question 32 The initial rate for an enzyme-catalyzed reaction has been determined at several substrate concentrations. Data are as follows: The Km value (µM) is: TT [S] umol/L v[(umol/L) min-1] 22 10 39 20 65 50 102 100 120 200 135 Select an answer and submit. For keyboard navigation, use the up/down arrow kéys to select an answer. a 800 100 1200 2000 e 90 10
Question 03 Write the inhibitors of following metabolic pathways 1. glycolysis 2. TCA
QUESTION 2 ADP AG"=-18.9 kJ/mol 1,3-Bisphosphoglycerate → 3-Phosphoglycerate Normal free energy of the shown step of glycolysis coupled with synthesis of one molecule of ATP is -18.9 kJ/mol. Calculate AG" (in kJ/mol) of dephosphorylation of 1,3-Biphosphoglycerate if AG"¹ of synthesis of ATP from ADP is 1.75. ATP AG" = 1.75 kJ/mol
Question 1. Answer the following questions: A. The complete oxidation of 1 mole of glucose to CO2 and H2O yields 686 kcal of free energy.How many ATP molecules could maximally be generated from one molecule of glucose, if theuseful chemical energy available in the high energy phosphate bond of 1 mole of ATP is 12kcal? B. However, it is known that cellular respiration produces 30 moles of ATP from 1 mole ofglucose. How does this compare with your answer in part (A)? Estimate the overall efficiency ofATP production from glucose? C. Assume that the cells of your body are oxidizing glucose and no energy is being dissipated asheat to the environment. However, the heat not converted into chemical-bond energy isincreasing the temperature of your body. How much would the temperature of your body riseupon oxidation of 1 mole of glucose if your body consists of 75 kg of water. [Hint: One kilocalorie (kcal) is defined as that amount of energy that heats 1 kg of water by 1oC]

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