4. The figure below shows ATP in the binding site of pyruvate kinase, an important enzyme incellular respiration. Note that only amino acids involved in interactions in the binding site areshown.LysHisATPNH; afafaforOH OHqatGluTyrAspa. What is the most likely chemical interaction occurring between the tyrosine and theribose of ATP?b. List one mutation to the lysine (Lys) in the binding site that would likely result in thekinase NOT being able to bind ATP (state the change in amino acid, not in the DNA ormRNA). In one sentence, explain why this mutation would likely lead to this change. Beas specific as possible.

Cellular respiration is a collection of three metabolic pathways that generate ATP by the oxidation…

Answered: 4. The figure below shows ATP in the…

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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One of the reasons for oxidizing the disulfide bonds in RNase A before removing the urea in the Anfinsen experiment was to demonstrate that ... Urea promotes disulfide bond exchange O Incorrectly-folded proteins lose their enzymatic activity. Urea prevents disulfide bond formation. Urea forms thio-esters with reduced cysteines at pH 8.2 Disulfide bonds are required for enzyme activity.
2. Consider the following quaternary cartoon structure below, where each colored shape represents a different subunit. i. ii. iii. How many N-termini are there in this complex? Suppose the blue square and orange triangle subunit are held together by a disulfide bond, sketch below what you would expect to see after the addition of BME. What kind of interactions may be responsible for holding the orange triangle and green circle subunits together? List at least three.
on -f ion Substituting antisense oligonucleotide non-bridging oxygen atoms with a sulpha atom: Select one: O a. Decreases oligonucleotide stability in biological fluids O b. Increases oligonucleotide hydrophobicity increasing the likelihood of it partitioning a O c. None of these Od. Increases oligonucleotide stability in biological fluids Oe. Has no effect on oligonucleotide stability in biological fluids Therapeutic replacement genes need to be delivered to which intracellular compartment? Select one: O a. The chloroplast O b. The lysosome The Nucleus O c. O d. The ribosome O e. The Golgi Give both answer only with little bit explanation Asap Thanks
5) The disease Phenylketonuria (or PKU) occurs when the enzyme that helps to catalyze the conversion of the amino acid phenylalanine into non-harmful tyrosine is mutated and doesn't work as well (or at all). Phenylalanine will still break down into tyrosine by itself, because this is a favorable reaction. Why is the non-functional enzyme a problem? Explain in a few sentences. al.H.colbe91srtihot wolsd sldu non lom i anolterineon mundillups betsmus 8880
7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 Rate constants (k's) for the reverse reactions are: k-1, k-3, K.4, k.6, and k.7 Write the enzyme balance for this mechanism. How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)
I only need a
In the first cycle of fatty acid synthesis via the acyl carrier protein system, the acetyl group on fatty acid synthase condenses with the malonyl-ACP complex. Draw the structure of the products of this reaction. Respresent ACP by R1 do not include free synthase Be sure to include charges on atoms at Ph=7
1. Glycosphingolipids function via cis regulation and trans recognition. Explain these terms and provide examples of each.
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.
7. An enzyme is discovered that catalyzes the chemical reaction : SAD + HAPPY A team of motivated researchers sets out to study the enzyme, which they call happyase. They find that the kcat for happyase is 600 s -1 and carry out several additional experiments. When [Et] = 20 nM and [SAD] = 40 µM, the reaction velocity is 9.6 µM s-1. Calculate KM for the substrate SAD. 8. In a separate enzyme happyase experiment using [Et] = 10 nM, the reaction velocity is measured at 3 µM s-l. What is the [S] used in this experiment?
8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.

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