Textbook Question
Which of the following reactions can be catalyzed by a decarboxylase?
a.
b.
Ch.19 Enzymes and Vitamins
McMurry8th EditionFundamentals of General, Organic, and Biological ChemistryISBN: 9780134015187
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Table of contents
- Ch.1 Matter and Measurements27
- Ch.2 Atoms and the Periodic Table20
- Ch.3 Ionic Compounds8
- Ch.4 Molecular Compounds23
- Ch.5 Classification & Balancing of Chemical Reactions12
- Ch.6 Chemical Reactions: Mole and Mass Relationships28
- Ch.7 Chemical Reactions: Energy, Rate and Equilibrium64
- Ch.8 Gases, Liquids and Solids24
- Ch.9 Solutions52
- Ch.10 Acids and Bases25
- Ch.11 Nuclear Chemistry22
- Ch.12 Introduction to Organic Chemistry: Alkanes57
- Ch.13 Alkenes, Alkynes, and Aromatic Compounds47
- Ch.14 Some Compounds with Oxygen, Sulfur, or a Halogen50
- Ch.15 Aldehydes and Ketones45
- Ch.16 Amines42
- Ch.17 Carboxylic Acids and Their Derivatives57
- Ch.18 Amino Acids and Proteins82
- Ch.19 Enzymes and Vitamins63
- Ch.20 Carbohydrates44
- Ch.21 The Generation of Biochemical Energy65
- Ch.22 Carbohydrate Metabolism45
- Ch.23 Lipids42
- Ch.24 Lipid Metabolism33
- Ch.25 Protein and Amino Acid Metabolism24
- Ch.26 Nucleic Acids and Protein Synthesis45
McMurry8th EditionFundamentals of General, Organic, and Biological ChemistryISBN: 9780134015187Not the one you use?Change textbook
Chapter 19, Problem 4b
Describe the reactions that you would expect these enzymes to catalyze.
b. Aspartate transaminase
Verified step by step guidance1
Understand the role of aspartate transaminase: This enzyme is a type of aminotransferase, which catalyzes the transfer of an amino group from one molecule to another. Specifically, aspartate transaminase facilitates the transfer of an amino group from aspartate to α-ketoglutarate.
Write the general reaction catalyzed by aminotransferases: Aminotransferases typically follow the reaction format: . For aspartate transaminase, the amino acid is aspartate, and the keto acid is oxaloacetate.
Identify the substrates and products: In the reaction catalyzed by aspartate transaminase, the substrates are aspartate and α-ketoglutarate. The products are oxaloacetate (a keto acid) and glutamate (an amino acid).
Describe the mechanism: The reaction involves the enzyme binding to aspartate and transferring its amino group to α-ketoglutarate. This process occurs via a Schiff base intermediate, where the enzyme's cofactor, pyridoxal phosphate (PLP), plays a critical role in facilitating the transfer.
Summarize the biological significance: Aspartate transaminase is crucial in amino acid metabolism and the urea cycle. It helps maintain the balance of amino acids and intermediates in metabolic pathways, such as the citric acid cycle.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Transamination
Transamination is a biochemical process that involves the transfer of an amino group from an amino acid to a keto acid. This reaction is crucial for amino acid metabolism and the synthesis of non-essential amino acids. Aspartate transaminase (AST) specifically catalyzes the transfer of an amino group from aspartate to alpha-ketoglutarate, producing oxaloacetate and glutamate.
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Enzyme Function
Enzymes are biological catalysts that speed up chemical reactions in the body by lowering the activation energy required for the reaction to occur. Each enzyme is specific to a particular substrate and reaction, which means that aspartate transaminase will only catalyze reactions involving aspartate and specific keto acids. Understanding enzyme function is essential for predicting the outcomes of biochemical reactions.
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Metabolic Pathways
Metabolic pathways are series of interconnected biochemical reactions that occur within a cell, leading to the conversion of substrates into products. Aspartate transaminase plays a key role in the amino acid metabolism pathway, linking amino acid catabolism and the citric acid cycle. Recognizing how these pathways interact helps in understanding the broader implications of enzyme activity in metabolism.
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Related Practice
Textbook Question
Identify and describe the chemical change in the lyase-catalyzed reaction in Table 19.4 that involves fumarate and malate. Identify the substrate(s) and product(s).
Textbook Question
The cofactors NAD+, Cu2+, Zn2+, coenzyme A, FAD, and Ni2+ are all needed by your body for enzymatic reactions.
a. Which cofactors are coenzymes?
Textbook Question
Name the enzyme whose substrate is
a. Urea
1
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