4.35ll LTE OQuestion 51 ptsWatch how the enzyme doesthe chemical reaction. Without thisenzyme, the substrate can't turninto the broken product!ProductsLook at the picture below anddescribe the enzyme-catalyzedreaction.SiteEnzyme-substratecomplexEnzymeProductEnzyme1. The substrates bond to theenzyme'sproduct2. A structure known as an"enzyme-substrate complex" isformed when they are connected.3. The enzyme has turned thesubstratęs into a(n)[ Select ]

These are multiple choice questions.

Answered: 1. The substrates bond to the enzyme's…

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 15TYK

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An enzyme contains an active site aspartic acid with a pKa = 5.0, whichacts as a general acid catalyst. On the accompanying template, draw thecurve of enzyme activity (reaction rate) versus pH for the enzyme (assumethat the protein is stably folded between pH 2–12 and that the active siteAsp is the only ionizable residue involved in catalysis). Briefly explain theshape of your curve.
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…
An enzyme has a maximal Velocity of 110.36 uM/s. At a substrate concentrationof 8.5 uM/s. What is Km in uM? Thank You!
1. Can the absorbance readings be used as a measure of enzyme activity atdifferent pH’s? 2. Describe an industrial application in which control of temperature and pHare critical to optimal enzymatic function.
26. AN ORGANIC COFACTOR IN A CONJUGATED ENZYME?A. NEITHER VITAMINS NOR MINERALSB. MINERALS C. VITAMINSD. BOTH VITAMINS AND MINERALS 27. WHICH OF THE FOLLOWING STATEMENTS CONCERNING COFACTORS IS INCORRECT?A. VITAMINS CANNOT BE COFACTORSB. SOME COFACTORS ARE METAL IONS C. COFACTOR IS THE NON-PROTEIN PORTION OF ENZYME D. CONJUGATED ENZYMES CONTAIN COFACTORS 28. WHICH OF THE FOLLOWING VITAMINS IS NOT A FAT SOLUBLE VITAMIN? A. VITAMIN E B. VITAMIN C C. VITAMIN A D. VITAMIN D 29. WHAT HAPPENS TO SUBSTRATE MOLECULES AT AN ENZYME ACTIVE SITE?A. ALWAYS REACT WITH OXYGEN B. UNDERGO CHANGE TO A DESIRED PRODUCTS C. BECOME CATALYST C ALWAYS REACT WITH OXYGEN B UNDERGO CHANGE TO A DESIRED PRODUCT D. BECOME COVALENTLY BONDED TO THE ENZYME D. BECOME COVALENTLY BONDED TO THE ENZYME 30. ACTION OF CHEMICAL WARFARE AND ORGANOPHOSPHATE INSECTICIDE ARE BASED ON?A. REVERSIBLE ENZYME INHIBITOR B. IRREVERSIBLE ENZYME INHIBITOR C. REVERSIBLE ENZYME ACTIVATOR D. IRREVERSIBLE ENZYME ACTIVATOR
What's the difference between the ordenary enzyme, inducable enzyme and allosteric enzyme according to enzyme kinetics?
1)Catalase a. Is catalase activity endothermic or exothermic? b. What classification of enzyme is catalase? c. Give the Enzyme Commission (E.C.) number of catalase. d. Is catalase reusable? answer all and don't copy from other sources I will downvote for sure
3.18: An enzyme E binds a substrate S and a cofactor C. The equilibrium dissociation constantKd,S of the enzyme-substrate complex ES is 1 μM, for EC it is 10 μM. When the cofactor Cis present, K’d,S is decreased to 0.1 μM. What is the value for the dissociation constant K’d,C of the enzyme-cofactor complex in the presence of substrate S? Calculate the interactionenergy ΔΔGint for cofactor and substrate binding.
1. Explain why the maximum initial reaction rate cannot be reached at low substrate concentrationsPredict or describe the absorbance or enzyme activity at: pH = 2 pH = 14 Explain your predictions 2. Explain why the maximum initial reaction rate cannot be reached at low substrate concentrations.
Q1. We plan a farge scale purification of enzyme using a packed colum of polyacrylamide beads. We obtain the following data, in a bed. of volume. 201t Volume Eiuted (iters) ‘Concentration (Arbitrary Units] 126 00073 40 00162 (maximum) Find the yieid at 150 lites eluted.
Which of the following substances does not participate in the CalvinBenson cycle? a. ATP b. NADPH c. RuBP d. PGAL e. O2 f. CO2
Describe the position of the transition state on a vertical energy scale, from low to high, relative to the position of the reactants and products, for both endergonic and exergonic reactions.

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1. The substrates bond to the enzyme's product 2. A structure known as an "enzyme-substrate complex" is formed,when they are connected. 3. The enzyme has turned the substratęs into a(n) [ Select ]