19) Why do enzymes have compact structures? (If enzymes weren't globular, then where would the non-polar sidechains be?)
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- Reminder: Enzymology is foundational to biochemistry. You should review and be familiar with the enzymes unit from BICH410. Here is a sample question as review!! Which of the following characteristics is(are) accurate in describing a regulated enzyme? Select all that apply. a) always responds the environment by covalent modification by phosphorylation b) displays only negative cooperativity c) contains multiple subunits d)has a defined T state and R stateBSC1010C 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.Answer the ff. questions: 1. To which class does each enzyme belong? Explain your answers. a.) pyruvate decarboxylase b.) alanine aminotransferase c.) alcohol dehydrogenase d.) hexokinase 2. Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis? 3. Some plants contain compounds that inhibit serine proteases. It has been hypothesized that these compounds protect the plant from proteolytic enzymes of insects and microorganisms that would damage the plant. Tofu, or bean curd, possesses these compounds. Manufacturers of tofu treat it to eliminate serine protease inhibitors. Why is this treatment necessary?
- AM Fri May 21 Take Quiz Coenzymes function to O denature the enzyme, stopping the chemical reaction from occurring. interact directly with enzymes, either enabling the reaction to occur or making the substrate-enzyme interaction more efficient. O change the shape of enzymes, allowing different additional substrates to bind. O dilate blood vessels, allowing more blood to flow, allowing more substrate to reach enzymes. O absorb excess hydrogen and hydroxide ions, keeping the pH relatively stable, so that reactions can occur most efficiently. Question 11 1 In the digestive system, which major organ starts the breakdown of proteins? O Mouth O Large intestines O Small intestines O Stomach O Esophagus Question 12 energy is energy found in the bonds of ingested nutrients.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…Challenge question 1: Calculate the number of ATP that will be CH. H-C-coo produced if a microorganism makes use of the following as substrate: HO-C-H socitrate coo NAD ase NADH co, • Lactate Coo glutarate CH, • Succinate čoo NAD COA • Malate
- 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.Q6 For the following pairs of molecules, identify the type of reaction (oxidation-reduction, hydrolysis, isomerization, or group transfer) required to convert the molecule on the left to the molecule on the right. In each case (6a-d), indicate the cofactor(s) or reactants that would be required, and any other products that would result. 6a R-CH,-CH2-CH2-C-S-CoA R—CH, — СН-СН-С—S-CoA O Palmitoyl-CoA O trans-A²-Enoyl-CoA 6b 6c но но но но + + H H H3N-C-C–0~ + H3N–C-Ĉ-0- H3N-C-C-N-C-C-0- Н-С—ОН H CH3 H H CH3 Glycine Alanine Н-С—ОН C=0 Glycylalanine НО —С—Н НО —С—Н Н-С—ОН Н-С—ОН 6d OH Он Он OH о он Н-С—ОН Н-С—ОН || | CH — С—СH2 CH2–C-CH2 CH2OH CH2OH H Glucose Fructose Glycerol Dihydroxyacetonewill UPVOTE!Kindly answer the following questions. What is an enzyme? How enzymes are being classified and enumerate its classification? How enzymes determine their substrate? What are the factors that affect enzyme activities?
- Q14. The transition state is an important intermediate that can influence the rate of an exergonic reaction. Which of the following statements about the transition state is correct? A. At the transition state reacting molecules are the most stable. B. The more molecules that can reach the transition state the faster the reaction will be. C. The transition state increases in the presence of an enzyme. D. If the transition state is high enough the reaction can move from being exergonic to being endergonic.14) Which of the following statements is true under the conditions provided: the enzyme concentration is 0.5 nM, substrate concentration is 10 µM, and the KM = 20 µM? a) The enzymatic reaction occurs at maximal velocity. b) The enzymatic reaction occurs between half-maximal and maximal velocity. c) The enzymatic reaction occurs at around half-maximal velocity. d) The enzymatic reaction occurs at between zero and half-maximal velocity. e) Not enough information given to know about the enzymatic reaction rate.Practice Mira Gendy 1 of 1 Directions: This short free-response question requires about 6 minutes to answer. The question is worth 3 points. Read the question carefully and completely. Answers must be written out in paragraph form. Outlines, bulleted lists, or diagrams alone are not acceptable. II Substrate Concentration [S] The graph above shows the initial rate of an enzyme-catalyzed reaction at different substrate concentrations in the presence of a constant concentration of the enzyme. Connect the primary structure of the enzyme to its overall shape. I U x X2 5 Initial Rate of Reaction