Given the active site and reaction mechanism below, what is the mechanism ofirreversible inhibition of the inhibitor provided?NH*Active Site*H₂N.HNNH₂+H₂NHNH₂N NH₂*Non-specific inhibitionUncompetitive InhbitorTransition State AnalogiAffinity-based inhibitionMechanism-Based InhibitionReaction Mechanism*H₂N.NHHN-HN[*]H₂N NH₂2+MnMn²+i+H₂N.H₂NiH₂N NH₂HOInhibitor*H₂N.BOHrView site informati

Irreversible inhibition is a process in which inhibitors bind covalently or non-covalently to a…

Answered: Given the active site and reaction…

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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Similar questions

Drug D reversibly binds to enzyme E and inhibits its activity toward substrate S. D binds equally well whether or not S is bound. Sketch a graph of the expected 1/v vs. 1/[S] relationship for: A) The enzyme reacting with S in the absence of drug D, B) The enzyme reacting with S in the presence of a small amount of drug D, and C) The enzyme reacting with S in the presence of a large amount of drug D.
The inhibitory effect of an uncompetitive inhibitor is greater at high [S] than at low [S]. Explain this observation.
Describe experimental enzyme inhibition and how it leads to a deeper understanding of enzyme mechanisms. Explain mechanism-based enzyme inhibition. Describe enzyme inhibition by a transition-state analog. For fluoroacetate and hypoglcyin A, explain how each of these mechanism-based inhibitors is converted to the actual enzyme inhibitor and how this inhibitor then inhibits the relevant enzyme..
The natural enzyme is recreated by mixing isolated regulatory and catalytic subunits of ATCase. What biological relevance does this observation have?
How can competitive and pure noncompetitive inhibition be distinguished in terms of KM?
The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo = Vmax [S] aKm + a' [S] where Vo is initial velocity, Vmax is maximum velocity, [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches/Vm Vmax 2α' Derive an expression for the effect of a reversible inhibitor on apparent Km from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. = Apparent, or observed, Km is equivalent to the [S] at which Vo max. apparent Km =
Does the presence of an uncompetitive inhibitor increase / decrease the apparent affinity of the enzyme•substrate complex?Does the apparent KM increase / decrease in the presence of an uncompetitive inhibitor?
One of the hallmarks of competitive inhibition is that there is constant competition betweenthe substrate and the inhibitor for binding to the enzyme active site.a) If [inhibitor] >> [substrate], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?b) If [substrate] >> [inhibitor], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?
What is the relative inhibition of an enzyme by a competitive inhibitor at [S] = KS and [I] = KI?
In a Lineweaver-Burk plot of an enzyme inhibited with a competitive inhibitor, how does the plot change with increasing inhibitor concentration? a) the slope decreases and the y-intercept stays the same b) the slope increases and the y-intercept stays the same c) the slope decreases and the y-intercept increases d) the slope increases and the y-intercept descreases e) none of the above
What is the difference between competitive and non-competitive inhibition? How can each be reversed?

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Given the active site and reaction mechanism below, what is the mechanism of irreversible inhibition of the inhibitor provided?