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Ch.19 Enzymes and Vitamins
Chapter 19, Problem 25.2

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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Step 1: Understand the biochemical pathway involved in the conversion of tryptophan to serotonin. This process involves two main steps, each catalyzed by a specific class of enzyme.
Step 2: Identify the first step in the conversion process. Tryptophan is first converted to 5-hydroxytryptophan. This reaction is typically catalyzed by a hydroxylase enzyme, specifically tryptophan hydroxylase, which belongs to the class of oxidoreductases.
Step 3: Recognize the role of oxidoreductases. These enzymes catalyze oxidation-reduction reactions, where the substrate is oxidized by the addition of an oxygen atom.
Step 4: Identify the second step in the conversion process. 5-hydroxytryptophan is then decarboxylated to form serotonin. This reaction is catalyzed by an enzyme known as aromatic L-amino acid decarboxylase, which belongs to the class of lyases.
Step 5: Understand the function of lyases. These enzymes catalyze the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Monoamine Neurotransmitters

Monoamine neurotransmitters are a class of neurotransmitters that include serotonin, dopamine, and norepinephrine. They are derived from amino acids and play crucial roles in regulating mood, emotion, and various physiological functions. Understanding their structure and function is essential for grasping how they influence brain activity and behavior.

Tryptophan

Tryptophan is an essential amino acid that serves as a precursor for serotonin synthesis. It must be obtained through diet, as the body cannot produce it. The conversion of tryptophan to serotonin involves specific enzymatic reactions, highlighting the importance of dietary intake in neurotransmitter production and overall mental health.
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Enzymatic Catalysis

Enzymatic catalysis refers to the process by which enzymes accelerate biochemical reactions. In the context of serotonin synthesis, specific enzymes catalyze the conversion of tryptophan through two distinct steps. Understanding the role of these enzymes is crucial for comprehending how neurotransmitter levels are regulated in the body.
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Related Practice
Textbook Question

Why are irreversible enzyme inhibitors referred to as poisons?

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Textbook Question

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?

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Textbook Question

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?

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Textbook Question

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.

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Textbook Question

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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Textbook Question

What are the cellular advantages to feedback inhibition?

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