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To what classes do the following enzymes belong? (a) Pyruvate decarboxylase (b) Chymotrypsin (c) Alcohol dehydrogenase

Short Answer

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(a) Lyases, (b) Hydrolases, (c) Oxidoreductases.

Step by step solution

01

Identify the enzyme classes

To determine the class to which each enzyme belongs, recall that enzymes are classified based on the general type of reaction they catalyze. There are six main classes.
02

Analyze enzyme name: Pyruvate decarboxylase

'Pyruvate decarboxylase' typically involves the removal of a carboxyl group from pyruvate, which is characteristic of the class of enzymes known as lyases. Lyases 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.
03

Analyze enzyme name: Chymotrypsin

'Chymotrypsin' is a well-known protease, which means it catalyzes the cleavage of peptide bonds in proteins. Enzymes that hydrolyze peptide bonds are classified as hydrolases, which catalyze reactions that involve the cleavage of bonds by the addition of water.
04

Analyze enzyme name: Alcohol dehydrogenase

'Alcohol dehydrogenase' catalyzes the oxidation of alcohols, typically using NAD+ as a cofactor to accept electrons. This reaction type is characteristic of oxidoreductases, which catalyze oxidation-reduction reactions.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Decarboxylases
Decarboxylases are a unique group of enzymes that facilitate the removal of a carboxyl group from organic molecules. This reaction usually results in the production of carbon dioxide as a product.
In the case of pyruvate decarboxylase, it acts on pyruvate to release carbon dioxide, which is a crucial step in various metabolic pathways, such as fermentation.
- These enzymes play a significant role in the citric acid cycle and in the anaerobic pathway of alcoholic fermentation. - The main function of decarboxylases is the decarboxylation process, which leads to the breakdown of carboxylic acids. Decarboxylases are incredibly important for the energy production processes in cells by helping to channel carbon atoms from metabolites.
Proteases
Proteases are enzymes that are specialized in facilitating the breakdown of proteins. They achieve this by hydrolyzing peptide bonds within proteins and peptides. Chymotrypsin is a classic example of a protease.
Proteases fall under the hydrolase class because they catalyze reactions through the addition of water, effectively cleaving bonds: - These enzymes are crucial in many physiological processes, including digestion, immune response, and cell regulation. - By breaking down proteins into peptides and amino acids, proteases play a vital role in protein metabolism and recycling. Proteases are used in many industries, such as pharmaceuticals and food processing, due to their ability to specifically target peptide bonds.
Oxidoreductases
Oxidoreductases are enzymes that catalyze oxidation-reduction reactions, often involving the transfer of electrons between molecules.
Alcohol dehydrogenase is a prime example of an oxidoreductase, catalyzing the reversible oxidation of alcohols into aldehydes or ketones: - This enzyme uses cofactors, such as NAD+ or NADP+, to transfer electrons. - Alcohol dehydrogenase is important in the metabolism of alcohols within the body, performing crucial roles in processes like fermentation and respiration. These enzymes are fundamental to many biochemical processes, including cellular respiration where they facilitate the transfer of electrons in the electron transport chain, crucial for ATP production.
Hydrolases
Hydrolases are enzymes that break chemical bonds through the addition of water, a process commonly known as hydrolysis.
They cover a broad category of enzymes including proteases, esterases, and phosphatases: - Hydrolases are responsible for breaking down complex molecules into simpler ones, which can be further utilized by the body. - The digestive process heavily relies on hydrolases, such as amylase and lipase, to break down carbohydrates and fats. By catalyzing bond cleavage with water, hydrolases play essential roles in both catabolic and anabolic pathways, supporting functions ranging from nutrient digestion to DNA repair.
Lyases
Lyases are enzymes that catalyze the breaking of various chemical bonds through mechanisms other than hydrolysis and oxidation.
These reactions often result in the formation of a new double bond or a new ring without using high amounts of energy. - Lyases help in bonding or breaking down molecules, creating small molecules necessary for different metabolic pathways. - Unlike hydrolases, lyases do not incorporate water into the substrate when breaking bonds. These enzymes play a significant part in metabolic processes that include the synthesis and breakdown of amino acids and other key biological molecules, contributing to cellular structure and energy dynamics.

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Most popular questions from this chapter

Show how you could use the acetamidomalonate method to prepare the following amino acids: (a) Leucine (b) Tryptophan

Proteins can be cleaved specifically at the amide bond on the carboxyl side of methionine residues by reaction with cyanogen bromide, \(\mathrm{BrC}=\mathrm{N}\). The reaction occurs in several steps: (a) The first step is a nucleophilic substitution reaction of the sulfur on the methionine side chain with BrCN to give a cyanosulfonium ion, \(\left[\mathrm{R}_{2} \mathrm{SCN}\right]^{+} .\) Show the structure of the product, and propose a mechanism for the reaction. (b) The second step is an internal \(S_{N}^{2}\) reaction, with the carbonyl oxygen of the methionine residue displacing the positively charged sulfur leaving group and forming a five-membered ring product. Show the structure of the product and the mechanism of its formation. (c) The third step is a hydrolysis reaction to split the peptide chain. The carboxyl group of the former methionine residue is now part of a lactone (cyclic ester) ring. Show the structure of the lactone product and the mechanism of its formation. (d) The final step is a hydrolysis of the lactone to give the product shown. Show the mechanism of the reaction.

What kinds of reactions do the following classes of enzymes catalyze? (a) Hydrolases (b) Lyases (c) Transferases

Evidence for restricted rotation around amide CO-N bonds comes from NMR studies. At room temperature, the \({ }^{1} \mathrm{H}\) NMR spectrum of \(N, N\) dimethylformamide shows three peaks: \(2.9 \delta\) (singlet, \(3 \mathrm{H}\) ), \(3.0 \delta\) (singlet, \(3 \mathrm{H}\) ), and \(8.0 \delta\) (singlet, \(1 \mathrm{H}\) ). As the temperature is raised, however, the two singlets at \(2.9 \delta\) and \(3.0 \delta\) slowly merge. At \(180^{\circ} \mathrm{C},\) the \({ }^{1} \mathrm{H}\) NMR spectrum shows only two peaks: \(2.95 \delta\) (singlet, \(6 \mathrm{H}\) ) and \(8.0 \delta\) (singlet, \(1 \mathrm{H}\) ). Explain this temperature-dependent behavior.

Cysteine is the only amino acid that has \(\mathrm{L}\) stereochemistry but an \(R\) configuration. Make up a structure for another L. amino acid of your own creation that also has an \(R\) configuration.

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