Discussion 11 enzyme kinetics and energetics F23 key

Activity 1: Practice Problems 1. In humans, phenylketonuria (PKU) is a disease caused by an enzyme deficiency at step A in the following simplified reaction sequence, and alkaptonuria (AKU) is due to an enzyme deficiency in one of the steps summarized as step B: A B phenylalanine tyrosine CO₂ + H₂O A person with PKU marries a person with AKU. What phenotypes do you expect for their children? wildtype O PKU O AKU O Both PKU and AKU

OCPS Das X ← → CO PS Login OCPS + Orders - X Performance Matters Question 12 of 16 Rate of reaction Previous Performa X olaocps.performancematters.com/ola/ola.jsp?clientcode=flocps# Join a Game - Quizizz K! Play Kahoot! - Enter... V C Educator X 19 Exam: 01 × Plans for X Submit Test Figure 1. Enzyme Rate of Reaction X = point of saturation The diagram below shows the relationship between substrate concentration and reaction rate. Dashboard ↑ Increasing concentration does not affect reaction rate AP EL U.S. Citize X F https://sex Performance Matte... S FLVS Login Welcome, Asheley! 02.Cl.Biology.CRM3.2_2023 4JypvK8X X + OT QMy Quizzes - Quizizz Athletic Clearance Substrate concentration Based on the graph, which of the following describes why continually increasing substrate does not lead to a continuous increase in reaction rate?

9:34 AM You sent       Help me with this one Select true if the statement is CORRECT and false if OTHERWISE   1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical…

Question: Please help me explain why tubes 1 and 3 showed evidence of unhydrolyzed strach after 30 minutes. Procedure and data sheet are already given

Question: what is the action of acid and alkali on the enzyme in saliva? Acid: Alkali:   (Procedure and data are already given)

Please show work/answer for 1 (a-c)

Please show all work/answers for 1 (d-g)

Module 5 Week 1 Assignment: Enzymes. This is a group assignment. You must work with a partner. Please be sure to have joined a group in Canvas and then upload one file for the group. The following kinetic data were obtained for an enzyme in the absence of inhibitor (1) or in the presence of two different inhibitors (2 and 3). The Enzyme concentration was the same in all of the experiments. Graph these data as a Lineweaver-Burke plot. Enzyme mM Inhibitor 2 [S] 1 Inhibitor 3 2 4 8 12 Enzyme (1) 12 20 a. Paste a photo of your Linewaver-Burke plot here. Plot all three lines on one graph. b. Using the date, fill in the following table; 29 35 40 v (umol/ml *sec) Inhibitor (2) 4.3 8 14 21 26 Vmax Km Apparent Vmax Apparent Km Type of inhibition Apparent Vmax Apparent Km Type of inhibition Inhibitor (3) 5.5 9 13 16 18 Click or tap here to enter text. Click or tap here to enter text. Click or tap here to enter text. Click or tap here to enter text. Click or tap here to enter text. Click or tap…

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URGENT

Question: Determine the Km and Vmax for this enzyme/substrate combination. [Substrate] (mM)                           V0 (mM/min)             0.25                                         0.183             0.50                                         0.356             1.00                                         0.665             2.50                                         1.45             5.00                                         2.35 What is the concentration of substrate necessary to achieve a turnover rate of 1.00 mM/min?

Study problem 2 4. A coworker has just isolated a copper enzyme that catalyzes the conversion of oil sludge into soluble alcohols in the presence of O₂. There are two Cu atoms per protein, which consists of a single polypeptide chain. As the bioinorganic chemist on the project, you are given unlimited quantities of the protein for the purpose of determining the active site structure. You have at your disposal a number of physical techniques, including NMR and EPR spectrometers, a magnetic susceptometer, a Mössbauer instrument, an X-ray absorption beam line, a UV-VIS spectrophotometer, a Raman spectrometer, a magnetic circular dichroism instrument, but, alas, no X-ray diffractometer. You have time to complete measurements by only three techniques before you have to give a report to your colleague. Describe what measurements you would make, in what order you would make them to get the most out of time, what results you might expect, and how you would use this information to characterize…

Answer for the number 3 question, Thank you.

Biochemistry topic question: An enzyme catalyzes a reaction with a with a Km value of 1 × 10–6 M and V max =20mmol/min. At a concentration of 1 × 10–6 M substrate, the rate of the reaction will be: See attached image. Please help. Thank you

Question:- For a simple enzymatic reaction that involves only one substrate and follows Michaelis–Menten kinetics, the changes in the concentrations of substrate, product, free enzyme, and the enzyme–substrate complex over the course of the reaction are depicted by solid curves in the graph below. Which curve (1 to 4) corresponds to [ES]? Write down the number as your answer.

Course Code: BIO121 Course Name: Principles of Biology I Read the question carefully first Answer the question-3(b) given chemical reaction according to the question (i) (ii) (iii) with step by step clear explanation. Enzyme X 3 (b) Given a chemical reaction: A + B- (i) (ii) (iii) Enzyme X can be used to catalyze the reaction above. Enzyme X binds to molecule A and B, and converts these molecules into product C. Using the lock and key model, explain how enzyme X is specific to its action. Predict what would happen to the rate of enzyme activity if the concentrations of molecule A and B are increased. Suggest ONE (1) way of how the activity of enzyme X can be controlled.

Pls help ASAP on both.

Topic: Co-Enzyme Q10   Question: What does it mean when asked to explain the evidence behind medicinal chemistry of the CAM agent, and if the chemical structures relate to it's effects.

Assignment Score: 77.9% Lx Give Up? E Feedback Resources Question 8 of 28 Complete these Brønsted-Lowry reactions. reaction 1: H, PO, + H* = H, PO Incorrect reaction 2: H., PO, + OH = PO + H,O Incorrect 9%6 e

Free Energy Practice Problems Determine the Free Energy & Spontaneity for each scenario A enthalpy (kl/mol) A entropy U/K) A Free Energy (kl/mol) Ender- or exergonic? Reaction Spontaneous or not? A +B > AB +12 -5 CD > C+D -32 +25 CH4+ 202> CO2+ -890 -243 2H:0 Nz+ 3H2 > 2NH3 -92 -199 Hydrolyzing ATP → ADP + P -0.31 Phosphorylation of Glucose (glucose + P) +14 2cOCl2 + Hz0 > CO2 -223 +284 + 2HCI *** ***Phosgene, COCI2, was used as a weaponized gas during World War I. It reacts with moisture in the lungs to produce HCI, which causes the lungs to fill with fluid, leading to death. Use the energy values above, at a body temp of 37°C (310K) to see if this reaction is spontaneous or not.

Biochemistry problem: Please help with problem in the attached image. The following information is associated with the question. Shown in the attachment is the enzyme activity for enzyme A. The measurements are made at severaldifferent substrate concentrations. What is the approximate value for the Km for this enzyme? Please help. Thank you

Need help with question number 2

I’m reviewing Enzyme Inhibition and am having issues wrapping my head around non-competitive and uncompetitive inhibition (and their consequent effect on Vmax / Km.)

answer item no. 7-10

Question:- 4. What product in this metabolic pathway could feedback to inhibit the pathway? What type of inhibition? 6. What is the sign of Delta G in Step "3" and "6"

Problem 1: Calculate the hydrolysis of ATP at pH 7 at 37°C under steady state conditions in which the concentration of ATP, ADP and Pi are maintained at 10-³M, 10 M and 10-2M, respectively. The AG' of hydrolysis of ATP at pH 7 = -32,217 J/mole, R = 8.314 JK ¹mol-¹, T= 273 + 37 K. ATP ADP + Pi

C7 Q6:

PROBLEMS 8.1 An enzyme-catalysed reaction was found to be affected by two inhibitors A and B. The following results were obtained at fixed total enzyme čoncentration: Substrate conc" Initial velocity (absorbance units per minute) (mmol l-) With 1 mmol I-IB Uninhibited With 1 mmol I-1À 50 20 0.684 1.08 0.653 1.01 0.649 0.476 0.374 0.311 10 1.43 0.468 1.02 0.363 0.296 3.3 0.798 2.5 2.0 0.657 0.549 0.250 Comment on these results.

Biochemistry topic question: An enzyme (A to B dehydrogenase) catalyzes the biochemical reaction A → B. Which ofthe statements found in the attached image is true? Please help . Thank you

Dropdown Choices 1. a) 20  b)10  c)30 2. a) 10  b) 5   c) 20  d) 2

Answer for the number 4 question, Thank you.