Q2An enzyme-catalyzed reaction has a Km-0.145 mM. Upon the use of a competitive inhibitor, the apparentKm 0.290 mM. The value of a rounded to the nearest whole number is:Given that 0.4 mM ofinhibitor was added to the reaction, what is the Ki of the inhibitor in mM, rounded to one significant digit(e.g. 0.5): You are trying to confirm that an enzyme you are studying has the following amino acid in its active site,and that this amino is critical for catalysis:HSOHNH₂Which of the following inhibitors could you use to provide evidence of the importance of this amino acidfor enzyme function?Nevirapinelodoacetate2,3-ButanedioneTetranitromethaneDiethylpyrocarbonate

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Answered: Q2 An enzyme-catalyzed reaction has a…

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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UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?
Only a few amino acid residues are actually involved in catalysis in enzymes, yet enzymes are constructed of at least 100 amino acids, and often many more. Suggest some functions for the noncatalytic amino acids.
Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed.
What are enzymes? What distinguishes enzymes from regular chemical catalysts? On the specificity of enzyme action, please comment. Which factor accounts for their specificity the most? Describe the enzyme catalysis mechanism.
When studying the mechanism of the enzymatic reaction, functional groups were found that ensure the connection of the enzyme molecule with the substrate and take a direct part in the act of catalysis. What are these areas of the enzyme formed by these groups called? What functional structures form them and why?
The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and other acyl esters. Name the amino acid residue, the side chain of the residuee and the type of bonding/linkage involved in the formation of the acyl-enzyme complex during catalysis.
Explain why the very tight binding of a substrate to an enzyme is not desirable for enzyme catalysis, whereas tight binding of the transition state is desirable.
The active site of an enzyme has the following amino acid residues as critical mediators of catalysis: Ser-134, His-347, Tyr-121 and Glu - 406. What are the most likely specific mechanisms of catalysis by these amino acid residues?
The glycine cleavage system is a group of four enzymes that together catalyze the following reaction: Use the following information to determine the sequence of reactions carried out by the glycine cleavage system:a. The first enzyme is a PLP-requiring decarboxylase.b. The second enzyme is aminomethyltransferase. This enzyme has a lipoate coenzyme.c. The third enzyme synthesizes N5,N10-methylene-THF and also forms +NH4.d. The fourth enzyme is an FAD-requiring enzyme.e. The cleavage system also requires NAD+ .
Give a complete and well descriptive definition of the following:1.1 Enzyme catalysis1.2 Co-enzyme1.3 Negative heterotropic co-cooperativit
Suicide substrates are substances that resemble the substrate,but when incorporated into the active site they form a covalent bond with the enzyme, permanently inhibiting it. Thesemolecules have been used to label the amino-acid side chainsthat are involved in the catalytic reaction occurring withinthe active site. This is usually accomplished by hydrolyzingthe inhibited enzyme. How could an investigator identify theamino acid bound to the suicide substrate molecule?
How is it possible to determine the structure of an enzyme substrate complex by x ray crystallography when the reaction is over so quickly and the x ray analysis takes at least several minutes?

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