19. The following is a plot of enzyme activity as a function of pH:Percent activity (%)050100567PHAssuming that there are only two titratable groups on the protein(and none on the substrate), give a likely explanation for theshape of this curve. Include in your answer the names of aminoacids that are likely to be involved and their protonation states.

Explanation for the Curve Shape:Low Activity Below pH 3: At very low pH values, both groups are…

Answered: 19. The following is a plot of enzyme…

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

The pKa for histidine is pKa = 6.1 while that for cysteine is pKa = 8.0 2. Assume that both histidine and cysteine are catalytic groups for a particular enzyme. Assume also that the side chain of cysteine must be in the deprotonated form. Estimate the pH at which the catalytic activity of this enzyme is the maximum and sketch a pH-activity graph.
A generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.
Calculate your dilution strategyto make a 625 ng/mLHRP solution from a 12.5 μg/mL stock given the totalvolume of enzyme youwillneed for your condition this week. Note if you are testing pH, you only need to calculate one enzyme dilution because all other pHs will use the same strategy.
Protease is an enzyme that catalyzes the breaking of amide bonds which is very stable at “mild” conditions, namely body temperature and pH 7 (if done in the lab requires hot conditions, concentrated HCl for hours). Some proteases have two aspartic acid residues at their active sites. Write the reaction mechanism (which follows general acid-base catalysis)
Please don't provide handwritten solution ....
In many biochemical reactions which involves the formation of an enolate intermediate, the carbonyl oxygen of the substrate is coordinated to a divalent metal ion (usually zinc or magnesium) in the active site. Explain with structural drawings, how this ion-dipole interactions affect the acidity of the a-protons?
Studies at diff erent pH’s show that an enzyme has two catalytically important residues whose pKs are ∼4 and ∼10. Chemical modifi cation experiments indicate that a Glu and a Lys residue are essential for activity. Match the residues to their pKs and explain whether they are likely to act as acid or base catalysts.
The enzyme lysozyme hydrolyzes glycosidic bonds in peptidoglycan, an oligosaccharide found in bacterial cell walls. The active site of lysozyme contains two amino acid residues essential for catalysis: E35 and D52. Which of the following statements about lysozyme is true? More than one may apply The graph shows the pH-activity profile of lysozyme. 100 50 4. 6. 8. 10 pH Residue E35 exhibits general base catalysis O The pKa of E35 is approximately 4.3 O The pKa of D52 is approximately 4.5 O The optimal activity of lysozyme is approximately 5.2 Residue E35 exhibits covalent catalysis The pka of E35 is approximately 6.1 The pka of D52 is approximately 3.7 Activity (% of maximal)
1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios
10) The graph shown below is the pre-steady state data for the serine protease (chymotrypsin) enzyme. Explain how this result suggests the formation of a covalent enzyme intermediate in the active site during the first step in the pathway. 3.0 2.0 1.0 1 3 Time (min) p-Nitrophenol (mol/mol of enzyme) 2.
With regards to arganine illustrate the pH-dependent transitions on a titration graph from most to least protonated. Indicate also the relevant part of the amino acid which is associated with the transition on that part of the graph.
After determining the optimum pH, you are now tasked to determine the inhibitory effects of acarbose, a known anti-diabetic drug which acts an inhibitor of alpha-glucosidase, an intestinal enzyme that hydrolyzes starch to release glucose for absorption and energy usage of the body. You studied the rates of the enzyme at different glycogen concentrations with and without the presence of 0.10 mM acarbose. Below is the summary for this procedure. a) What is the Vmax, in arbitrary units, of the uninhibited reaction (without acarbose)? b) What is the KM , in mM, of the uninhibited reaction (without acarbose)? c) What is the type of inhibition?

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