1.Shown below is a metabolic pathway:EsEE4E1E2A - B - C - DE3E6Q- R – SE7EsSuppose we have too much of "S" in the cell, please answer the following questions, with regards to feedbackinhibition:a)Which enzyme is most likely to be regulated?b)Which substance will act as the 'regulator'?c)Name the "site" where this 'regulator' will bind to the enzyme:d)Is this substance (from #b), a homotropic or heterotropic modulator?

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Answered: 1. Shown below is a metabolic pathway:…

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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Zymogens are NOT enzymatically active, because O A. they are not yet shaped such that essential proximity and orientation catalysis can occur. B. the active site amino acids have been mutated. O C. they have not yet bound the proper cofactor D. they are always smaller than active enzymes.
OOC H H fumarase Fumarate S-malate What class of enzyme most likely catalyzes the reaction shown in the figure? choose the one best answer) Oxidoreductase COO H₂O HR IIII... Hs OOC OH COO IIIH
Which of the following describes a purpose for the function of phosphoglucoisomerase? a) allows for phosphorylation for trapping the molecule in the cell b)promotes substrate level phosphorylation and formation of ATP c) allows formation of a primary alcohol necessary for the next step of phosphorylation d)facilitates epimerization, the change in stereochemistry at one chiral carbon
There are many metabolic pathways in a biological system, and it is critical to regulate these pathways so that only particular pathways are active at a single time. Which enzyme would be in the regulation point in the hypothetical pathway shown below. A¹B 2C 3 D4E A) A → B B) B-C C) C-D D) D→ E E) The regulation point is highly dependent upon the metabolic pathway.
19
Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acety/A-ase Acetate - A-ase Deacetylase A-ase Protease & C-ase B-ase ABCD What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback Inhibition 1
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)
Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
The 2 eynzymes are affected by a substrate. Choose all correct answers.
5. Enzymes are incredibly effective at facilitating chemical reactions and must be controlled- or the chemical reaction won't stop and the reactant(s) might be used up. (A) Use 3 different colors to color the coding circles and corresponding structures in the figures. (B) Draw an arrow pointing to the active site in each figure. (C) Beneath each diagram, write the type of inhibition and briefly, in your own words, explain what is happening. PG al JartW Mool bluow nolsoeen er edw gni nobisvitae ert wori gniworla en qsp/ru to can't S uid can't weib (A) wole Ts w.bind b (8) bris bobl ewm bind oll omysne erlf yd beoue o.gons O Enzyme O Reactant (substrate) O Inhibitor Enzyme Enzyme Type of inhibition: Type of inhibition:
2. “Most enzymes are gene-encoded proteins." Using this lens, explain: A) effects of increased temperature on the rate of enzymatic reactions, and B) effects of decreased temperature on enzymatic reactions, and C) importance of optimal pH and ionic strength on enzymatic reactions.
1. A metabolic pathway proceeds according to the scheme, R → S →T→U→ V→ W. A regulatory enzyme, X, catalyzes the first reaction in the pathway. Which of the following is most likely correct for this pathway? A) Either metabolite U or V is likely to be a positive modulator, increasing the activity of X. B) The first product S, is probably the primary negative modulator of X, leading to feedback inhibition. C) The last product, W, is likely to be a negative modulator of X, leading to feedback inhibition. D) The last product, W, is likely to be a positive modulator, increasing the activity of Х. E) The last reaction will be catalyzed by a second regulatory enzyme.

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