31.A) What is the overall order of an enzymatic reaction, under conditions where thesubstrate concentration is much higher with respect to KM? Assume Michaelis-Mentenbehavior.a) zerob) firstc) secondd) thirde) disordered31.B) What is the order of an enzymatic reaction with respect to the substrate,under conditions where the substrate concentration is much higher with respect toKM? Assume Michaelis-Menten behavior.a) zerob) firstc) secondd) thirde) disordered

Km is the Michaelis menton constant which is equal to Substrate concentration at which the velocity…

Answered: 31.A) What is the overall order of an…

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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14) Which of the following statements is true under the conditions provided: the enzyme concentration is 0.5 nM, substrate concentration is 10 µM, and the KM = 20 µM? a) The enzymatic reaction occurs at maximal velocity. b) The enzymatic reaction occurs between half-maximal and maximal velocity. c) The enzymatic reaction occurs at around half-maximal velocity. d) The enzymatic reaction occurs at between zero and half-maximal velocity. e) Not enough information given to know about the enzymatic reaction rate.
In a Lineweaver-Burk graph, the lines representing the uninhibited and inhibited enzyme catalyzed reaction meet each other on the x-axis. The type of inhibition which is occurring is: a) competitive b) noncompetitive c) uncompetitive d) allosteric CO2 exerts direct activity upon hemoglobin by: a) blocking oxygen from binding to the heme group b) displacing BPG from the central cavity c) oxidizing Fe+2 to Fe+3 which does not bind oxygen d) forming an N-terminal carbamate which favors the T-state The dominant motif found in hemoglobin and myoglobin is: a) helix-turn-helix b) twisted beta sheet c) beta barrel d) random coil Which of these is an ketohexose? a) fructose b) glucose c) ribose d) erythrose Which of these is a constitutional isomer of d-glucose? a) fructose b) galactose c) l-glucose d) ribose Which of these is an enantiomer of d-glucose? a) d-fructose b) d- galactose c) l-glucose d) d-ribose Which of these is a diastereomer of…
13.) An unchanged apparent Km results from the action of an uncompetitive inhibitor because A) the presence of the inhibitor can shift the binding equilibrium toward the ES complex. B) the presence of the inhibitor can shift the binding equilibrium toward the E + S state. C) the presence of excess substrate shifts the binding equilibrium toward the ES complex. D) uncompetitive inhibitors do not alter the binding equilibrium between substrate and enzyme. E) Uncompetitive inhibitors always result in a lower apparent Km, not an unchanged apparent Km.
9) Considering the enzymatic reaction catalyzed by HIV protease: Options A) hydrolysis is the net reaction observed. B) a peptide bond is cleaved on the carboxyl side of a proline residue. C) a serine residue serves as the nucleophile during the catalytic event. D) inhibitors have been designed to covalently link to the active site just like natural substrates do. E) None of the above is true. F) All of the above are true.
Which of the following catalyzes reactions that incorporate nitrogen derived from glutamine? a) Glutamine synthase b) Glutamine amidotransferase c) Adenylyltransferase d) Glutamate synthase
D) What are the different substrate specificities of elastase, trypsin, and chymotrypsin? And, why, from a structural standpoint, do elastase, trypsin, and chymotrypsin have different substrate specificities?
Based on the kinetic constants below, which enzyme will most efficiently catalyze conversion of the substrate into product? A) Vmax = 10 uM s-1, KM = 10 µM B) Vmax = 10 uM s-1, KM = 0.01 µM C) Vmax = 1000 uM s-1, KM = 500 µM D) Vmax = 1 uM s-1, KM = 1 µM E) Vmax = 200 uM s-1, KM = 10 µM
Where do each of these 5 main themes occur in the chymotrypsin mechanism? 1) substrate specificity 2) induced fit 3) covalent catalysis 4) acid/base catalysis 5) transition state stabilization
1. In a catabolic pathway, metabolite X gets converted into metabolite Y, metabolite X 0 J mol-¹ and AG' is <0 J mol-¹ for this reaction. a) At standard states, is this reaction favorable? b) Is the reaction favorable or unfavorable at cellular condition? c) Is this an endergonic or exergonic reaction in the cell? d) Would you describe this as a thermodynamically downhill or uphill reaction in the cell?
which of the following functions matches with the coenzyme functions: a.) facilitate redox reaction in the anabolic pathway b.) carry acyl group via a thioester bond c.) facilitate redox reaction involving C=O in the catabolic pathway d.) facilitate redox reaction involving C=C CoEnzymes to pair the functions from: NAD+ FAD NADP+ Coenzyme A
You perform Michaelis-Menten kenetics on i) trypsin and ii) a mutant form of the same enzyme (a single amino acid has been changed). The specificity constant for the mutant was 10 times larger than for trypsin. a) Define the specificity constant and explain using this definition how a larger value might occur. b) Explain how, if at all, a non-competitive inhibitor of trypsin would affect the specificity constant.
Statins are competitive inhibitors that target HMG CoA reductase to decrease plasma cholesterol. a) What effect statin has on the enzyme's Km, b) How can we reverse a competitive inhibitor's effect? a) Increases Km, b) Increasing the [S] a) decreasing Km, b) Increasing the [S] a) Increases Km, b) decreasing the [S] a) No effect on Km, b) Inhibitor cannot be reversed

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