BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
9th Edition
ISBN: 9781319425746
Author: BERG
Publisher: MAC HIGHER
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Chapter 24, Problem 27P
Interpretation Introduction
Interpretation:
Feedback mechanism for the given pathways, such that, Y and Z production is the same.
Concept introduction:
A feedback inhibition is a process in which the product of any reaction acts as the regulator of the reaction itself. By this, the production of the product gets limited. In this mechanism, the product binds to the allosteric site of the enzyme, and changes the shape of the active enzyme, resulting in loss of activity of the enzyme.
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I. Active site analysis.
Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of
tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation
to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid
architecture of an active site is designed to bind substrates. Amino acid side chains are capable of
hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is
suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0
a.a.#1
a.a.#2
a.a.#6
HO
Lond
NH₂
НО
a.a.#5
OH
a.a.#3
a.a.#4
1F. Please help me in detail. for molecular Mechanism of ATP versus GTP selectivity of adenylate kinase, Draw a reaction scheme that includes both the substrate and the inhibitor under study here. Be sure to label KI, Ks, kp
1G. Please help me in detail. For Molecular Mechanism of ATP versus GTP selectivity of adenylate kinase,
Write an expression for the reaction velocity.
Chapter 24 Solutions
BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
Ch. 24 - Prob. 1PCh. 24 - Prob. 2PCh. 24 - Prob. 3PCh. 24 - Prob. 4PCh. 24 - Prob. 5PCh. 24 - Prob. 6PCh. 24 - Prob. 7PCh. 24 - Prob. 8PCh. 24 - Prob. 9PCh. 24 - Prob. 10P
Ch. 24 - Prob. 11PCh. 24 - Prob. 12PCh. 24 - Prob. 13PCh. 24 - Prob. 14PCh. 24 - Prob. 15PCh. 24 - Prob. 16PCh. 24 - Prob. 17PCh. 24 - Prob. 18PCh. 24 - Prob. 19PCh. 24 - Prob. 20PCh. 24 - Prob. 21PCh. 24 - Prob. 22PCh. 24 - Prob. 23PCh. 24 - Prob. 24PCh. 24 - Prob. 25PCh. 24 - Prob. 26PCh. 24 - Prob. 27PCh. 24 - Prob. 28PCh. 24 - Prob. 29PCh. 24 - Prob. 30PCh. 24 - Prob. 31PCh. 24 - Prob. 32PCh. 24 - Prob. 33PCh. 24 - Prob. 34PCh. 24 - Prob. 35PCh. 24 - Prob. 36PCh. 24 - Prob. 37PCh. 24 - Prob. 38PCh. 24 - Prob. 39PCh. 24 - Prob. 40P
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Draw TCA Cycle. Please make sure to state all the enzymes and co-factors for each step of the pathway.arrow_forwardNeed help, please.arrow_forwardA7. Consider what can be concluded about the catalytic site (substrate binding site) of phosphatase and the binding site of NaF from the type of inhibition shown by NaF for phosphatase and illustrate it schematically. The inhibition typre is pure noncompetitive inhibition.arrow_forward
- Need help, please.arrow_forward1H. please help me in detail. For molecular Mechanism of ATP versus GTP selectivity of adenylate kinasearrow_forwardA. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)arrow_forward
- Pls answer all. I'll give like.arrow_forwardSelect all that apply. What is true about the conformational aspects of coupling? O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change. O The conformational states interconvert as a result of proton flux through the synthase. There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T). Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis. The Fo portion of ATP synthase acts as a rotary motor.arrow_forwardPlease do all .arrow_forward
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