Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- Allosteric regulation plays a very important role in the regulation of glycogen metabolism. Which of thefollowing is correct? -AMP allosterically inhibits glycogen phosphorylase -Glucose-6-phosphate allosterically activates glycogen synthase -Both A and B -Neither A nor B The value of standard free energy change for reaction A --> B is +3.7 kJ/mol. Under which of thefollowing conditions, the reaction will most likely become exergonic in the direction as written? -Mass action ratio is larger than the equilibrium constant -Couple with ATP hydrolysis -Both A and B -Neither A nor Barrow_forwardn your own words and with your own diagrams, describe the catalytic reaction mechanism of the enzyme acetylcholinesterase. Discuss the functional roles of each member of the catalytic triad plus whatever other residues that you find important. Describe the actual movements of protons, and the making and breaking of bonds. What types of chemistries is the enzyme using? (what is the enzyme doing, in term of reactionarrow_forwardTrend observed in graph and conclusion about the effect of temperature on enzyme activity. i) include a concise description of the trend observed in the graph shown in question 3 above, and explain this trend using the language presented in this unit and your biochemical knowledge of enzymes and reactions. In your conclusion, provide a logical argument supported by molecular theory that would explain any change observed in enzyme activity.arrow_forward
- Help with "d" through "h"arrow_forwardWhich of these processes is most exergonic? (Think VERY carefully!) Dephosphorylation of glucose Conversion of enol to keto Oxidation of an aldehyde to a carboxylic acid group. ATP hydrolysisarrow_forwardTrend observed in graph and conclusion about the effect of temperature on enzyme activity. In your answer i) include a concise description of the trend observed in the graph shown , and ii) explain this trend using the language presented in this unit and your biochemical knowledge of enzymes and reactions. In your conclusion, provide a logical argument supported by molecular theory that would explain any change observed in enzyme activityarrow_forward
- With a ∆G°´ of -16.7 kJ/mol, the reaction catalyzed by hexokinase is considered to be _____. at equilibrium substrate and product concentration dependent freely reversible metabolically irreversible none of the abovearrow_forwardGive the Steps, Enzyme/s involved, Electron carriers, ATP Generation, End product and significance of the following metabolic pathway: Kreb's Cycle (explain in 1-3 sentences only)arrow_forwardMAKE A GRAPH FOR ME ON GRAPH PAPER CALL IT ENZYMES VS RATE OF REACTION USING TABLE BELOW GRAPH paper INSERTED BELOW rules: data points must be an x or circled dot, must be on grid paper , the independant variable on the x axis and dependant variable on the y axis, must include titles Regarding the data points: - H2O2 + MnO2 Control #1: (Control #1, 5)- H2O2 + sand control #2: (Control #2, 0)- Plant versus Animal Liver Catalase: (Liver, 4)- Potato: Plant vs. Animal Catalase: (Potato, 3)- Substance Enzyme Concentration (Used Liver): (Liver Used, 4)- Substance Enzyme Concentration (Used H2O2): (Used H2O2, 1) - Boiling Water Bath Temperature: (Boiling Water Bath, 5)- Ice Water Bath Temperature: (Ice Water Bath, 2)- HCl, or pH 3: (H 3, 4)- NaOH at pH 12: (pH 12, 2)- pH 7 (H2O): (assuming average of pH readings; pH 7, not specified) The following explains how to display the graph: Title: Factors versus Enzyme Activity Rate - Labels on X- and Y-axes: Factors and Rate of Enzyme…arrow_forward
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