The rate of an enzyme catalysed reaction was measured with increasing substrate concentrations in the presence of 0 µM, 2 μM or5 μM of a non-reactive substrate analogue capable of binding to the active site. The following double reciprocal Lineweaver-Burkplot was produced from the data obtained. Match each of the following terms with the correct label (A-G) on the plotPrompts1/[5](B)(A)(c)(D)(E)(G)(F)AnswersSelect match2Select matchReaction with 2 μM of the substrateanalogue3-1/KMLast saved 10:26:12Questions Filter (16)Q SearchSelect matchKFirst Last >|公告MEDEThi10BE OF £ & 2 2 2 211.YouHaQuqubasheWOpe

Therefore:"1/S" = (F)"Reaction with 2 µM of the substrate analogue" = (B)"-1/Km" = (G)This makes…

Answered: The rate of an enzyme catalysed…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 10QP: b. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein...

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a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
MATHEMATICAL The enzyme -methylaspartase catalyzes the deamination of -methylaspartate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]. The rate of the reaction was determined by monitoring the absorbance of the product at 240 nm(A240). From the data in the following table, determine KM for the reaction. How does the method of calculation differ from that in Questions 26 and 27?
MATHEMATICAL The hydrolysis of a phenylalanine-containing peptide is catalyzed by -chymotrypsin with the following results. Calculate KM and Vmax for the reaction. PeptideConcentration(M)Velocity(Mmin1)2.51045.010410.010415.01042.21065.81065.91067.1106
MATHEMATICAL Catalase breaks down hydrogen peroxide about 107 times faster than the uncatalyzed reaction. If the latter required one year, how much time would be needed by the catalase- catalyzed reaction?
The Energy Cost of dTTP Synthesis (Integrates with Chapter 20.) Starting from HCO3, glutamine, aspartate, and ribosc-5-P, how many ATP equivalents are consumed in the synthesis of dTTP in a eukaryotic cell, assuming dihydroorotate oxidation is coupled to oxidative phosphorylation? How does this result compare with the ATP costs of purine nucleotide biosynthesis calculated in problem 2?
MATHEMATICAL For the Vmax obtained in Question 26, calculate the turnover number (catalytic rate constant) assuming that 131024mol of enzyme were used.
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.
MATHEMATICAL Predict the predominant forms of the amino acids from Question 8 at pH 10.

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