АCTIVITY 5.2.4Create a graph illustrating the activity of an enzyme or rateof reaction with the different factors affecting enzymeactivity: 1) concentration of enzyme, 2) concentration ofsubstrate, 3) temperature, 4) pH

The rate of reaction increases as the enzyme concentration rises. Because the rate of an…

Answered: Create a graph illustrating the…

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter6: Metabolism

Section: Chapter Questions

Problem 19CTQ: Describe the position of the transition state on a vertical energy scale, from low to high, relative...

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Enzyme Action: Testing Catalase Activity 8) Explain why the [VO] of the reactions at pH 3 and temperature of 100'C were (or should have been) tower than the other treatments conducted. In your response consider the following: a) The effect of these conditions on the structure of the enzyme. b) Why this structural effect resulted in a decreased [VO].
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 reaction catalyzed. 9. The living cell is the site of tremendous…
Result nad Discussion Lead Acetate Reaction: Samples: lysine, cysteine, methionine Reagents: 10% Sodium Hydroxide (NaOH) and Lead Acetate Pb(CH3COO)2 -To 1 ml of the amino acid solution taken in a test tube, add few drops of sodium hydroxide (40%) and boil the contents for 5-10 mins over a bunsen burner. Cool the contents and add few drops of 10% Lead acetate solution and observe.
Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…
. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.
1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:
BSC1010C Enzymes & Cellular Regulation Dr. Harris 4. Compare the rate of the pepsin-catalyzed reaction at pH = 1.5 with the rate of the lipase- catalyzed reaction at pH = 1.5. 5. Compare the rate of the pepsin-catalyzed reaction at pH = 8.0 with the rate of the lipase- catalyzed reaction at pH = 8.0. 6. Based on your understanding of protein structure, explain in detail the effect of exposing an enzyme to a pH outside its optimal range. Include a discussion of the effect on both the structure and function of the enzyme. 7. At what pH values is lipase likely to be denatured? Explain your answer.
2c which is altered by a catalyst such as an enzyme, the net free energy change of the reaction or the activation energy of the reaction?
Which of the following is not true about the premise of a dose/response relationship? 25 A There is a dose with maximum effect B) There are doses without effects Graded response depends on dose D LD50 is the inverse square of the dose
100 increasing enzyme ativity optimum pH 5 6 9 10 11 7 8 pH 20 40° 60°C Temperature 1. How do pH and temperature affect enzyme activity? 2. What do the graphs suggest about the activity of the enzyme? 3. Draw a graph that represents the role of enzymes in metabolism. (Rubrics on next page.)
I. Buffer Preparation A researcher in Biochemistry is isolating α-glucosidase enzyme from malted wheat flour. The protocol requires the use of 2.00L of 0.225 M of lactate buffer with pH of 4.25. How will he/she prepare this buffer from 2.00 M lactic acid solution and solid sodium lactate (NaC3H5O3) The Ka of lactic acid is 1.38 x 10-4. [ Na=23.0, C=12.0, H=1.01, O=16.0 g/mol]
I. Indicate whether each of the following statements are true or false. _1. According to the lock-and-key model of enzyme action, the active site of an enzyme is flexible in shape. 2. In an enzyme-catalyzed reaction, the compound that undergoes a chemical change is called the substrate. 3. The nonprotein portion of a conjugated enzyme is the enzyme's active site. _4. Simple enzymes have inorganic cofactors, and conjugated enzymes have organic cofactors. 5. Vitamins are required in minute quantities for normal cellular function. 6. vitamins are found in all food groups. 7. Ribose sugars are found on one chain of the DNA molecule and deoxyribose sugars are found on the other chain of the DNA molecule. 8. A DNA molecule has a double helix at one end of the molecule and a single helix at the other end of the molecule. _9. Complementary bases are held together by covalent bonds. 10. DNA molecules always contain the nitrogenous base thymine.

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Create a graph illustrating the activity of an enzyme or rate of reaction with the different factors affecting enzyme activity: 1) concentration of enzyme, 2) concentration of substrate, 3) temperature, 4) pH