Answer number 2-10. Which fill in the blanks only.Answer the number 4-5. Which multiple choice only.*NOTE THIS:NO NEED TO EXPLAIN EACH PROBLEM. JUST PEOVIDE A BEST ANSWERS TO IT.*PLEASE HELP ME OUT. I'M BEGGING YOU PLEASE.THANK YOU IN ADVANCE Direction: Provide the best answer in the blank.Feed back1. inhibition regulates the rate of many metabolic pathways.2.attach to the enzyme at an allosteric site.3.can bind to an enzyme's active site and compete with substrate.4.is a place on an enzyme where a molecule that is not a substrate may bind.Enzyme activity can be affected by a variety of factors, such as 5.7.8.and 9.6.10. Evidently the graph on a substrate concentration will present a Which interacts to hydrophilic and hydrophobic environments?a. proteinc. phospholipidWhich characteristic of a phospholipid contributes to the fluidity of the membrane?b. cholesterold. carbohydratea. its headb. cholesterola saturated fatty acid taild. double bonds in the fatty acid tailС.4.5.

Enzymes are biological catalysts that can accelerate the reaction rate and catalyze chemical…

Answered: Answer number 2-10. Which fill in the…

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Biology

Answer number 2-10. Which fill in the blanks only. Answer the number 4-5. Which multiple choice only.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 9TYK: Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric...

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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.
IDENTIFICATION: 1.In this model, the substrate still needs to fit into the enzyme like a key, but instead of simply fitting into the "keyhole," some type of modification is induced in the substrate, enzyme, or both. 2.Creatinine Kinase found in skeletal and heart muscle 3.Creatinine Kinase found in heart muscle 4.Creatinine Kinase found in the brain 5. To overcome an energy barrier between reactants and products, energy must be provided to get the reaction started. This energy, which is recovered as the reaction proceeds, is called: A. Potential energy B. Initiation energy C. Reaction energy D. Activation energy 6. The active site of the enzyme and substrate have complementary structures, hence they fit together as a key fits a lock. 7. TRUE or FALSE. Increase concentration of substrate, Increase enzyme action. 8. TRUE or FALSE. Decrease concentration of enzyme, Increase enzyme action.
2:51 Enzymes.pdf 7 of 8 Enzyme Active sites Substrates Enzyme substrate complex Enzyme is recycled Substrate modification Product C • Label the diagram on the following slide: • 1. substrates • 2. products • 3. energy of activation without enzyme • 4. energy of activation with enzyme • 5. Which has more energy in this reaction, the substrates or the products? • 6. What happens to the difference in energy during the reaction? How dees an enzyme make reaction go ster? a chemical A+B evergy Time (mim) Copyrighte T Jhe eya Son uaOLOGr TU S 22
Select all statements that are correct. Note there might be more than 1 correct statement. Competitive inhibitors bind to an allosteric side on the enzyme Uncompetitive inhibitors bind to the substrate binding site Competitive inhibitors bind to the substrate binding site Competitive inhibitors are usually of similar size and shape than the substrate of the enzyme Non-competitive inhibitors can bind to the free enzyme but not to the enzyme-substrate complex pe here to search C 6 D 88 20°C T ENG
Strategies to Regular Enzyme Activity: Give an example of an enzyme that uses the strategy shown and describe how the activity of the enzyme is regulated. Regulatory Strategy 1. Covalent Modification 2. Feedback Inhibition 3. Cascade of Reaction Enzyme Describe how the regulatory strategy is employed
Match the definition to the term: v Choose... Temporary molecule that is formed when substrate attaches to the enzyme Substrate Product Compound that enters the reaction Substance that functions as a biological catalyst Enzyme Specific portion of the enzyme where the substrate attaches Result of enzyme reaction Active Site Enzyme-substrate complex Choose...
Which statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.
Fill the blank with the option below The substrate concentration at which an enzyme-catalyzed reaction proceeds at on-half its maximum velocity The rate enhancement of the enzyme catalyzed reaction over uncatalyzed reaction The rate of the reaction when the concentration of the products is zero and the reverse rate is negligible The rate at which the enzyme-substrate complex is formed The number of time an enzyme molecule transforms a substrate molecule per unit of time The proportionality constant that relates the velocity of a chemical reaction to the concentrations of the reactants The maximum velocity of an enzymatic reaction when the binding site is saturate with substrate A measure of the catalytic activity of an enzyme at low concentrations of substrate The rate constant for the equilibrium between the reactants and the enzyme-substrate complex 1. Vo 2. 4. 3. V₁ Acronym Parameter 6. 7. I 5. Km 8. 1 I 9. AAG 10. AG rate constant rate of disappearance I specificity constant…
Which statement is NOT completely true? O In the Induced-fit theory, the conformation of the active site changes to accommodate an incoming substrate. O A urease which hydrolyzes only urea is an example of an enzyme that exhibits relative specificity. O Cofactors that are organic also go by the name coenzymes O Many enzymes require a second substance present (cofactor) in order to be active. O Enzymes are protein based catalysts. O Enzymes are sensitive to heat and pH O Enzymes catalyze at their "active site". O Apoenzymes are inactive enzymes.
3. Enzyme specificity. To determine the specificity of substrate binding for a particular enzyme/protein, structurally related compounds may be used as potential substrates and Km values may be calculated. However, many compounds structurally related to the substrate may bind to the active site but cannot be converted to product. In these instances, the substrate analogs are used as potential competitive inhibitors of substrate binding. Low K, values indicate high affinity of the enzyme for the inhibitor, whereas high K,values indicate low binding affinity. Consider the enzyme xanthine oxidase, which catalyzes the formation of uric acid from the purine bases hypoxanthine or xanthine in humans. The Km for hypoxanthine is 15.0 μM and for xanthine it is 45.0 μM. A few compounds used as competitive inhibitors of the normal substrate hypoxanthine are listed in the table below with their K; values. Comparing the structures of hypoxanthine with the listed substrate analogs, what can you…
5. By using Excel or GoogleSheets. graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Kwax values for the inhibited and uninhibited reactions? Is the inhibitor competitive or noncompetitive? [S] (mM) V, No Inhibitor (mmol min-) V, Inhibitor Present (mmol min-') 1 × 10-4 5 × 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 0.026 0.010 0.092 0.136 0.040 0.086 0.150 0.120 0.165 0.142
O D. Point of saturation 5. Idențify TRUE statement regarding the active site. * O A. A region that contains vitamins. O B. A region that binds the allosteric inhibitors. O C.A region with changing conformation. D. A region where bonds are formed between the substrate and the products. 6 Distinouish a term for a chemical reaction that has a positive AG