Fundamentals of General, Organic, and Biological Chemistry - With Access
8th Edition
ISBN: 9780134465708
Author: McMurry
Publisher: PEARSON
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Textbook Question
Chapter 19, Problem 19.52AP
How do you explain the observation that pepsin, a digestive enzyme found in the stomach, has a high catalytic activity at pH 1.5, while trypsin, an enzyme of the small intestine, has no activity at pH 1.5?
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Chapter 19 Solutions
Fundamentals of General, Organic, and Biological Chemistry - With Access
Ch. 19.1 - Prob. 19.1PCh. 19.1 - The enzyme LDH converts lactate to pyruvate. In...Ch. 19.2 - The cofactors NAD+, Cu2+, Zn2+, coenzyme A, FAD,...Ch. 19.3 - Describe the reactions that you would expect these...Ch. 19.3 - Prob. 19.5PCh. 19.3 - Prob. 19.6PCh. 19.3 - Prob. 19.7PCh. 19.3 - Prob. 19.8PCh. 19.4 - Prob. 19.9KCPCh. 19.5 - Prob. 19.10KCP
Ch. 19.5 - Prob. 19.11PCh. 19.5 - Prob. 19.12PCh. 19.6 - Prob. 19.13PCh. 19.6 - Prob. 19.14PCh. 19.7 - (a) L-Threonine is converted to L-isoleucine in a...Ch. 19.8 - AZT (zidovudine) inhibits the synthesis of the HIV...Ch. 19.8 - Prob. 19.3CIAPCh. 19.8 - Prob. 19.16PCh. 19.9 - Does the enzyme described in each of the following...Ch. 19.9 - Prob. 19.18PCh. 19.9 - Compare the structures of vitamin A and vitamin C....Ch. 19.9 - Prob. 19.20PCh. 19.9 - Prob. 19.21KCPCh. 19.9 - Prob. 19.22PCh. 19.9 - Prob. 19.4CIAPCh. 19.9 - Prob. 19.6CIAPCh. 19.9 - Prob. 19.7CIAPCh. 19.9 - Enzyme levels in blood are often elevated in...Ch. 19.9 - Prob. 19.9CIAPCh. 19.9 - Prob. 19.23PCh. 19 - Prob. 19.24UKCCh. 19 - Prob. 19.25UKCCh. 19 - Prob. 19.26UKCCh. 19 - Prob. 19.27UKCCh. 19 - Prob. 19.28APCh. 19 - Explain how the following mechanisms regulate...Ch. 19 - Prob. 19.30APCh. 19 - Prob. 19.31APCh. 19 - Prob. 19.32APCh. 19 - Prob. 19.33APCh. 19 - Prob. 19.34APCh. 19 - Prob. 19.35APCh. 19 - Prob. 19.36APCh. 19 - Prob. 19.37APCh. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - What features of enzymes make them so specific in...Ch. 19 - Describe in general terms how enzymes act as...Ch. 19 - Prob. 19.42APCh. 19 - Prob. 19.43APCh. 19 - Prob. 19.44APCh. 19 - Prob. 19.45APCh. 19 - Prob. 19.46APCh. 19 - Prob. 19.47APCh. 19 - What is the difference between the lock-and-key...Ch. 19 - Why is the induced-fit model a more likely model...Ch. 19 - Prob. 19.50APCh. 19 - Prob. 19.51APCh. 19 - How do you explain the observation that pepsin, a...Ch. 19 - Prob. 19.53APCh. 19 - Prob. 19.54APCh. 19 - Prob. 19.55APCh. 19 - Prob. 19.56APCh. 19 - Prob. 19.57APCh. 19 - The text discusses three forms of enzyme...Ch. 19 - Prob. 19.59APCh. 19 - Prob. 19.60APCh. 19 - Prob. 19.62APCh. 19 - Prob. 19.63APCh. 19 - The meat tenderizer used in cooking is primarily...Ch. 19 - Prob. 19.65APCh. 19 - Why do allosteric enzymes have two types of...Ch. 19 - Prob. 19.67APCh. 19 - Prob. 19.68APCh. 19 - Prob. 19.69APCh. 19 - Prob. 19.70APCh. 19 - Prob. 19.71APCh. 19 - Prob. 19.72APCh. 19 - Prob. 19.73APCh. 19 - Prob. 19.74APCh. 19 - Prob. 19.75APCh. 19 - Prob. 19.76APCh. 19 - Prob. 19.77APCh. 19 - Prob. 19.78APCh. 19 - Prob. 19.79APCh. 19 - Prob. 19.80CPCh. 19 - Prob. 19.81CPCh. 19 - Prob. 19.82CPCh. 19 - Prob. 19.83CPCh. 19 - Prob. 19.84CPCh. 19 - Prob. 19.85CPCh. 19 - Prob. 19.86CPCh. 19 - Prob. 19.87CPCh. 19 - Prob. 19.88GPCh. 19 - The ability to change a selected amino acid...Ch. 19 - Prob. 19.90GPCh. 19 - Prob. 19.91GP
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- Can same enzyme have different kinetics for different substrates? What is the biological significance that?arrow_forwardDo all enzymes display kinetics that obey the Michaelis– Menten equation? Which ones do not?arrow_forwardWhy 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.arrow_forward
- What are two major advantages of enzyme catalysts in living organisms when compared with other simple chemical catalysts such as acids or bases?arrow_forwardWhat does it mean to say that an enzyme- catalyzed reaction is either enzyme limited or substrate -limited?arrow_forwardAt what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?arrow_forward
- Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis?arrow_forwardWhy does the activation energy of a reaction not appear in the final Δ G of the reaction?arrow_forwardIf we describe an enzyme like aspartate transcarbamoylase and say that it exhibits cooperativity, what do we mean?arrow_forward
- You begin to study enzyme Z, which catalyzes a simple reversible reaction that interconverts compound S and compound P. You observe that the ∆G´° for the S to P conversion to be –6 kJ/mol, and that compound S has ∆G´° for binding to enzyme Z of –15 kJ/mol, while compound P has a ∆G´° for binding to enzyme Z of –13 kJ/mol. Please explain the effect of enzyme Z on conversion of S to P. (Your answer should include a graph qualitatively showing energy versus reaction progress; however, you still need to explain youranswer in words!) not sure how to make the correct graph.arrow_forwardWhat are the three key mechanisms and their associated features that are utilized by enzymes to catalyze reactions. Additionally, which two mechanims of the three you listed does the enzyme chymotrypsin use?arrow_forwardHow is it possible to determine the structure of an enzyme substrate complex by x ray crystallography when the reaction is over so quickly and the x ray analysis takes at least several minutes?arrow_forward
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