Why are irreversible enzyme inhibitors referred to as poisons?
Serotonin is a monoamine neurotransmitter. It is formed in the body from the amino acid tryptophan (Figure 28.6, p. 836). What class of enzyme catalyzes each of the two steps that convert tryptophan to serotonin?
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Verified Solution
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Key Concepts
Monoamine Neurotransmitters
Tryptophan
Enzymatic Catalysis
Apple slices and peeled potatoes rapidly brown in open air due to the presence of phenolases. Phenolases cause the oxidation of phenolic molecules like tyrosine to quinones, colored molecules responsible for the brown colors seen. An experiment comparing the time it took for a change to occur in the color of apple slices versus potato slices was done to test for phenolase activity. Then, a second experiment was done with new apple and potato slices with H2O2 measuring time until bubbles appeared. <IMAGE>
b. Which sample contains more catalase? Why?
The reaction that follows is catalyzed by isocitrate dehydrogenase and occurs in two steps, the first of which (step A) is formation of an unstable intermediates (shown in brackets).
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d. To what class of enzymes does isocitrate dehydrogenase, the enzyme that catalyzes this reaction, belong?
What type of enzyme regulation occurs in the following situations?
a. Buildup of the product of the pathway that converts glucose to pyruvate stops at the first enzyme in the multistep process.
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?
What are the cellular advantages to feedback inhibition?