Asp residue (both of which are essential for catalysis) with pK, values of 5.9 and 4.5, respectively. Ifthe enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and whichwill act as the general base during the initial steps of the reaction? Explain your reasoning. (

In simple terms, pH indicates whether a substance is acid or base. pKa determine how strong is an…

Answered: Asp residue (both of which are…

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

Draw two reaction coordinate diagrams (DG vs reaction coordinate) that compare the uncatalyzed process of lipid flipping (lipid out à lipid in ) from outer to inner leaflet to the flippase-catalyzed process.
RuBP carboxylase is by no means an ideal enzyme. Describe some of the problems with its active site and its substrate specificity. If we compare the amino acid sequences of this enzyme from many different species, they are almost identical. What is the significance of this uniformity?
A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)
Consider the dissociation reaction for a protein-ligand complex: P•L P + L A. Sketch a binding curve (fractional saturation θ vs. ligand concentration [L]) for this protein-ligand complex (ligand A). Show where on that curve you could obtain the dissociation equilibrium constant Kd for the reaction. B. Now sketch on the same axes a θ vs. [L] plot for a different ligand (B) that binds more weakly than the first ligand. C. Does the weaker binding ligand have a higher, or lower, Kd than the tighter binding ligand? D. Sketch a binding curve for a cooperatively bound ligand with K0.5 higher than that of Kd for A or B. (Note: for cooperative binding, each protein molecule would have to have more than 1 binding site for the ligand; K0.5 is the experimentally determined ligand concentration that gives θ = 0.5.)
Considering PNPP → PNP reaction, would you expect to see more intense or pale color for the reaction that contain the inhibitor? Explain.
The transport of aspirin (pKa = 3.5, structure shown here) from the digestive tract to the circulation occurs by nonmediated absorption into cells lining the stomach (where pH = 0.8) and the small intestine (where pH 6.0). Do you expect absorption to be faster in the stomach or in the small intestine?
Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
The reaction in which glucose 6-phosphate (G6P) is converted to fructose 6-phosphate (F6P) is an example of an isomerization reaction. Notice that both molecules have the molecular formula C6H13O9P. The isomerization is catalyzed by glucose 6-phosphate isomerase. This is a reversible reaction in cells, with a moderately negative ΔG, but a very high activation energy. If you have a flask that contains a solution containing cellular concentrations of G6P and F6P, but no enzyme, how will the concentration of each molecule change over time?
8L.16.2
An enzyme contains an active site aspartic acid with a pKa = 5.0, whichacts as a general acid catalyst. On the accompanying template, draw thecurve of enzyme activity (reaction rate) versus pH for the enzyme (assumethat the protein is stably folded between pH 2–12 and that the active siteAsp is the only ionizable residue involved in catalysis). Briefly explain theshape of your curve.
Can you please help show how to find Kr?

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