8L.16.4 The Michaelis-Menten parameters, kcat and KM, for selected enzymes are given in the table below. Use these parameters to determine the catalytic efficiency ofeach enzyme. Based on your calculations arrange the enzymes in increasing order of their efficiencies.EnzymeReactionCatalaseSubstrateH₂O2UreaseUreaAcetylcholinesterase Acetylcholine2-trans-enoyl-COACrotonaseTriose phosphateisomeraseGlyceraldehyde3-phosphateLowestRank from lowest to highest catalytic efficiency. To rank items as equivalent, overlap them.► View Available Hint(s)2H₂O2 + Catalase → 2H₂O + O2H₂N-C(=O)-NH2 +2H₂O + Urease → 2NH4+ + CO3²-Acetylcholine + Acetylcholinesterase acetate + choline2-trans-enoyl-CoA +Crotonase →→→ 3-hydroxyl-COA + H₂OGlyceraldehyde 3-phosphate + Triosephosphate isomerase → Dihydroxyacetone phosphate 4.3 × 10³ 4.7 × 10¯-4Crotonase Catalase Triosephosphate isomerase UreaseThe correct ranking cannot be determined.1.1kcat (S-¹) KM (M)4.0 × 1071.0 × 104 2.5 × 10-²1.4 x 104 9.0 × 10-5-25.7 × 10³ 2.0 × 10-5AcetylcholinesteraseResetHelpHighest

Km is a measure of enzyme affinity for the substrate. It measures the stability of the ES complex.…

Answered: The Michaelis-Menten parameters, kcat…

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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You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphatase
Although graphical methods are available for accurate determination of the Vmax and Km of an enzyme-catalyzed reaction, sometimes these quantities can be quickly estimated by inspecting values of V0 at increasing [S]. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained:
uizzes/67365/take Based on the image below, select the correct statements. Note: There may be more than 1 correct response. I Ribose 5-phosphate ribose phosphate pyrophosphokinase (PRPP synthetase) glutamine-PRPP amidotransferase adenylosuccinate synthetase AMP > 5-Phosphoribosylamine I adenylosuccinate PRPP lyase 9 steps Adenylosuccinate AMP IMP <-- ADP - AMP <-- GMP <-- IMP IMP dehydrogenase <- GMP - XMP ADP ATP GMP يمد XMP-glutamine amidotransferase Increased levels of ADP inhibit the production of PRPP. Increased levels of GMP inhibit the production of XMP. O Increased ADP activates PRPP synthase to increase PRPP levels. Increased IMP activates glutamine-PRPP amidotransferase to further increase IMP levels. 8 OBC
How to calculate the percent inhibition of xanthine oxidase enzyme inhibition with a blank absorbance value lower than the sample absorbance? Can the formula (Asample-A blank)/Asample ) x 100% be used? Thank you if you are willing to explain in detail Thank you.
A particular enzyme-catalyzed reaction has an apparent Vmax = 9.00 nmol s-1 and α' = 3.00 when 2.00 µmol L-1 inhibitor X is present and uncompetitively inhibiting the reaction. Calculate Vmax for the uninhibited reaction in nmol s-1.
The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis–Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect (no change, half as large doubles, increases, decreases) on the maximal velocity, Vmax, and Michaelis constant, KM, of the hypothetical enzyme.
Create a ONE page, formal summary, including APA Formatted in-text citations, of the enzyme amalyze and how it is used in the meat processing industry (Address all guiding questions below in your summary). Note, references can be the second page of the assignment. Include the questions in ur answer Which enzyme is used in the industry (if more than one enzyme is included, you can choose one of the enzymes) Describe the molecular structure of the enzyme (how many amino acids; discuss different levels of protein structure-secondary, tertiary, quaternary, key structural components/amino acids in active site) Describe how the enzyme works in the industry and why it is a key component for this industry. What specific reaction(s) are being catalyzed? What types of bonds are being broken?
Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
For the following aspartase reaction in the presence of the inhibitor hydroxymethylaspartate, determine Km and whether the inhibition is competitive or noncompetitive. You have to plot thegraph on the graph paper and also by using excel.[S] V, No Inhibitor V, Inhibitor Present(molarity) (arbitrary units) (same arbitrary units) 1 x 10-4 0.026 0.0105 x 10-4 0.092 0.0401.5 x 10-3 0.136 0.0862.5 x 10-3 0.150 0.1205 x 10-3 0.165 0.142
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
Studies were carried out to investigate some kinetic properties of alkaline phosphatase (ALP) extracted from Lepus townsendii liver. Incubation of ALP extract with 4- nitrophenylphosphate (4-NPP) formed the basis for determination of enzyme activity. Spectrophotometric method was used to assay the enzyme activity, and the kinetic constants- maximum enzyme velocity (Vmax) and Michealis-Menten constant (Km) were evaluated. Figure 2 shows the Lineweaver-Burk plot of ALP assay in the presence of inhibitor NaH;PO4 (0) and the control (+) analysis. [I]: concentration of inhibitor = 0.67 mM. 1/V, uM*min x 104 40- 30 20 y-Intercept 10 x-intercept -1/K. (1+ [1]/K)/ 12 1/[S)x 102 (M) Figure2 (i) Estimate Km and Vmax in the absence and presence of the inhibitor. (ii) What is the type of inhibition illustrated by the inhibitor? Explain.
Given the following data in enzyme-catalyzed reaction, what are the Vm, Km of with DEDS (presence of inhibitor) and without DEDS ( absence of inhibitor) and its type of inhibition.

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