An enzyme contains an active site aspartic acid with a pK, = 5.0,which acts as a general acid catalyst. On the template below, draw thecurve of enzyme activity (reaction rate) vs. pH for the enzyme(assume the protein is stably folded between pH 2–12 and that theactive site Asp is the only ionizable residue involved in catalysis).Briefly explain the shape of your curve. 10075502579.11pH% enzyme activity

Amino acids Proteins are the polymers of nitrogenous compounds called amino acids. Each amino acid…

Answered: An enzyme contains an active site…

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

Carboxypeptidase, which sequentially removes carboxyl-terminal amino acid residues from its peptide substrates, is a single polypeptide of 307 amino acids. The two essential catalytic groups in the active site arefurnished by Arg 145 and Glu 270 .(a) If the carboxypeptidase chain were a perfect α helix, how far apart (in Å) would Arg 145 and Glu 270 be? (b) Explain how the two amino acid residues can catalyze a reaction occurring in the space of a few angstroms
Why do structural analogs of the transition-state intermediate of an enzyme inhibit the enzyme competitively and with low Ki values (binds tightly)?
An organic chemist is generally happy with 95% yields. If you synthesized a polypeptide and realized a 95% yield with each amino acid residue added, what would be your overall yield after adding 10 residues (to the first amino acid)? After adding 50 residues? After 100 residues? Would these low yields be biochemically “satisfactory”? How are low yields avoided, biochemically?
Discuss the behavior of enzymes as described by the Michaelis-Menten Equation
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.
Histidine is frequently used as a general acid or base in enzyme catalysis. Considering the pKa value of the side chain, suggest a reason why is this so?
What is the smallest number of molecules of ATP and GTP consumed in the synthesis of a 200- residue protein, starting from amino acids? Assume that the hydrolysis of PP i is equivalent to the hydrolysis of ATP for this calculation.
Assume that some protein molecule, in its folded native state, has one favored conformation. But when it is denatured, it becomes a “random coil,” with many possible conformations. (a) If we only consider the change in entropy for the protein, what must be the sign of ∆S for the change: native → denatured? (Note: As suggested in the next problem, this does not include solvent effects, which also make significant contributions to ∆S.) (b) How will the contribution of ∆S for native → denatured affect the favorability of the process? What apparent requirement does this impose on ∆H if proteins are to be stable structures?
Let’s consider histidine as a free amino acid in aqueous solution. a) Draw the most likely structure of histidine under biochemical standard state conditions. b) Given that free histidine has the following three pKa values, assign each to its corresponding acidic hydrogen or conjugate base in your structure from part a). pKa1 = 1.7; pKa2 = 6.2; and pKa3 = 9.1 c) For each pKa, give the corresponding expression for the equilibrium constant. It helps to write out the chemical equation for each. d) Create a speciation diagram for histidine by plotting Xi vs pH from pH = 4 to pH = 8 where Xi is the mole fraction of the two histidine species involved in the K2 equilibrium in part c).
The breakdown of a complex carbohydrate into its monomeric unit can be described as an enzyme-catalyzed reaction that has a deltaG(∆G) of -90kcal/mol. Suppose you were to add triple the amount of enzyme into this reaction - what would be the ∆G of this reaction?
The activity of an enzyme requires a glutamic acid to display its -COOHfunctional group in the protonated state. Suppose the pKa of the -COOHgroup is 4.07.(a) Will the enzyme be more active at pH 3.5 or 4.5? Explain.(b) What fraction of the enzymes will be active at pH = 4.07? Explain.(c) At what pH will the enzyme show 78% of maximal activity?
Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein. please do not copy from other answers here

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