When substrate concentration [S] << Km, the rate of anenzymatic reaction is increased byO increasing kcat/KmO increasing total enzyme concentrationO increasing [S]O A and BO A, B and C

The enzymes are biological catalysts that increase the rate of biochemical reactions.The enzymes are…

Answered: When substrate concentration [S] << Km,…

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 21P

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Why Do Anabolic and Catabolic Pathways Differ? Why is the pathway for the biosynthesis of a biomolecule at least partially different from the pathway for its catabolism? Why is the pathway for the biosynthesis of a biomolecule inherently more complex than the pathway for its degradation?
Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
PREDICT In the following reaction series, which enzyme(s) is/are most likely to have an allosteric site to which the end product E binds? (a) enzyme 1 (b) enzyme 2 (c) enzyme 3 (d) enzyme 4 (e) enzymes 3 and 4
In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
Enzymes _______. a. enhance reaction rates b. are affected by pH c. act on specific substrates d. all of the above
Understanding the Mechanisms of Reactions Related to Transketolase The mechanistic chemistry of the acetolactate synthase and phosphoketolase reactions (shown here) is similar to that of the transketolase reaction (Figure 22.30). Write suitable mechanisms for these reactions.
Understanding the Mechanism of Hemolytic Anemia Genetic defects in glycolytic enzymes can have serious consequences for humans For example, defects in the gene for pyruvate kinase can result in a condition known as hemolytic anemia. Consult a reference to learn about hemolytic anemia, and discuss why such genetic defects lead to this condition.
Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
When glucose reacts with ATP to form glucose-6-phosphate: a. the synthesis of glucose-6-phosphate is exergonic. b. ADP is at a higher energy level than ATP. c. glucose-6-phosphate is at a higher energy level than glucose. d. because ATP donates a phosphate to glucose, this is not a coupled reaction. e. the reaction is spontaneous.
Imagine that you are working with isolated mitochondria and you manage to double the ratio of protons outside to protons inside. In order to maintain the overall Gat its original value (whatever it is), how would you have to change the mitochondria membrane potential?
Characterizing Glycolysis List the reactions of glycolysis that a. are energy consuming (under standard-stale conditions), b. are energy yielding (under standard-state conditions), c. consume ATP. d. yield ATP e. are strongly influenced by changes in concentration of substrate and product because of their molecularity. f. are at or near equilibrium in the erythrocyte (see Table 18.2).
Comparing Glycolysis Entry Points for Sucrose Sucrose can enter glycolysis by either of two routes: Sucrose phosphorylase: Sucrose + Pi fructose + glucose-1-phosphate Invertase: Sucrose + H20 fructose + glucose Would either of these reactions offer Jin advantage over the other In the preparation of hexoses fur entry into glycolysis?

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When substrate concentration [S] << Km, the rate of an enzymatic reaction is increased by O increasing kcat/Km O increasing total enzyme concentration O increasing [S] O A and B O A, B and C