1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysisexemplified by the serine protease: Chymotrypsin. In your answer discuss employingthe illustration whenever possible: the overall reaction mechanism, stability of thereaction transition state, proximity and orientation effects, acid-base catalysis, andcovalent catalysis.(c)(0)ApAsp ToeHisAsp 10C-N bond cleavageHNHoSerGerBinding ofsubsti196SerGlyalto videoLBHBNHSereHARProtondonationby H(h)Fel ofamino productyestOHNHigSerAp(0)Formation ofcovalent (ES)Alp MecomplexSerios

The active site of chymotrypsin consist of a combination of 3 specific amino acid residues that work…

Answered: 1. Please fully explain (use illustrate…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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.
24. Consider the figure below, which is an alternate way to depict the energy changes occurring during a reaction from Substrate (S) to Product (P), when uncatalyzed (curve A) and when catalyzed by an enzyme (curve B). Note that curve B is not the same way we modeled an enzyme-catalyzed reaction in class; this model is a different, perhaps slightly more realistic, way of conceptualizing the energy changes over the course of a reaction than what we did in class. S and ES represent the transition states for reaction of the free substrate (S) or the enzyme-substrate complex (ES). T T activation energy for uncatalyzed reaction EST S edhosob nohtum od bluo woH abiow yedio 2 wwolaixa-y odi no vaigin oroda dapng odt ni o nfog) r gibadhoa P B ES EP progress of reaction activation energy for catalyzed reaction a) Explain briefly why, in curve B, the energy state of the enzyme-substrate complex is less than the energy state of the substrate alone. b) Suppose the enzyme in the diagram was mutated…
1. Provide the best coenzyme(s) for each step shown below. Give a 1–2 sentence rationale for your choice. 2. Reaction (C) can require multiple coenzymes, or the enzyme may only require one. Briefly describe how the reaction that uses only one coenzyme works. Be specific about the mechanism.
please focus on this question 3 times i submitted it and three different answers, please make sure of ur answer
To investigate the effects of a newly discovered inhibitor and enzymology list obtained the results showed in the figure below. Which statement best describes the binding of its inhibitor on the enzyme? ~y=0.768r+4.7425 3-0.568x+46576 19 . . . . ● x X The inhibitor binds at the active site. The inhibitor binds away from the active site, but after substrate binding. The inhibitor binds away from the active site before or after substrate binding. The inhibitor binds close to the active site, but after substrate binding. The inhibitor binds close to the active site, but prior to substrate binding. red by a strain
enzyme-inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displays kinetics somehow similar to non-competitive inhibition, does this is inhibitor good to use to inhibit toxanthine oxidase in the case of hyperuricemia and gout?
6. Examine the plot of the enzyme-catalyzed reaction below: Wheat-germ acid phosphatase shows Michaelis-Menten kinetics when acting on para-nitrophenol phosphate 16 14 12 10 8 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 (S] / mM a) Is this reaction better characterized by Michaelis-Menten kinetics or simple mass action? b) What is the approximate value of Vmax? Km? c) Assuming that this plot was made at 100 nM enzyme, draw the curve, including axis labels, for 300 nM enzyme. d) Imagine that this enzyme is inhibited by a competitive inhibitor with Ki (for inhibitor) = Km (for substrate). Note that v = (kcat [E] tot [S]/Km) / (1 + [S]/Km + [I]/Ki). Draw the curve of reaction velocity (v) versus [S] for [I] = 1 mM. e) Now consider an experiment where you simultaneously introduce substrate and competitive inhibitor at equal concentrations. Make a plot of v versus concentration of [S] = [I], i.e. the X-axis should be the concentration of both I and S, which are equal. v/ uM min-
Please answer asap and in short
What enzyme kinetic parameters are apparantly impacted by uncompetitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor Vmax
Please answer this question and the highlighted question is wrong please explain why and give me the correct answer
How many of the following statements are true? Allosteric enzymes display sigmoidal kinetics for plots of V versus [S] Allosteric enzymes exist in T and R states Allosteric enzymes display kinetics that becomes less sigmoidal in the presence of activators
Kindly refer to the photo attached. thank you

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