4AI. Refer to the figure below and answer the following questions:45555665PH7758.5010B1520253035Temperature (°C)4045Legend: Blue - wild-type ß-galactosidase; Red - mutant ß-galactosidasea. What is the optimum pH of wild type ß-galactosidase?b. What is the optimum temperature of mutant ß-galactosidase?c. Which enzyme has the greater activity at pH 7.2?d. Which enzyme has the greater activity at a temperature of 42.5°C?e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4?f. Which enzyme has greater activity if temperature increases from 40°C to 41 °C?5055

Enzyme activity refers to the general catalytic activity of an enzyme. It can be affected by:…

Answered: a. What is the optimum pH of wild type…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 25P: Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the...

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There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…
38. Glycogen isolation 1. The liver is a major storage site for glycogen. Purified from two samples of human liver, glycogen was either treated or not treated with a -amylase and subsequently analyzed by SDS-PAGE and western blotting with the use of antibodies to glycogenin. The results are presented in the adjoining illustration on the next page. (a) Why are no proteins visible in the lanes without amylase treatment? (b) What is the effect of treating the samples with a - amylase? Explain the results. (c) List other proteins that you might expect to be associated with glycogen. Why are other proteins not visible?
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
How GTN works? What are the combination drug therapy are used in managing the hyperlipidemia? Please briefly explain at your own words.
#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
Lysozyme’s use of aspartic acid and glutamic acid, to break the glycosidic bonds of the eubacterial cell wall (composed of peptidoglycan), illustrates the common enzymatic pattern of: hydrolysis (catabolic), using nonpolar amino acids at the active site hydrolysis (catabolic), using polar amino acids at the active site condensation (anabolic), using nonpolar amino acids at the active site condensation (anabolic), using polar amino acids at the active site all of the above
Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). II. What is the net ATP yield for the complete oxidation of all the fatty acid residues of the simple TAG? (Note: glycerol backbone is not included)
Explain the biochemical functions and deficiency manifestation ofVit D ?
Legend: Blue – wild-type β-galactosidase Red – mutant β-galactosidase _________ a. What is the optimum pH of wild type β-galactosidase? _________ b. What is the optimum temperature of mutant β-galactosidase? _________ c. Which enzyme has the greater activity at pH 7.2? _________ d. Which enzyme has the greater activity at a temperature of 42.5oC? _________ e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? _________ f. Which enzyme has greater activity if temperature increases from 40oC to 41 oC?
What are the measures to inhibit the Maillard reaction in undesirable situations. please explain detailed
1C One of the major findings of this study is that GTP arrests the enzyme. Draw (i) the natural substrate ATP; (ii) the substrate analog, GTP, and (iii) the GMP-PCP molecule. Indicate where they are different. For each molecule, indicate where the hydrolysable (scissile bond) is located. Please help me
4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.

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