Podcast
Questions and Answers
What is the role of glutamate in the nitrogen metabolism process?
What is the role of glutamate in the nitrogen metabolism process?
- It is solely responsible for the transport of glucose to muscles.
- It serves as a precursor for gluconeogenesis.
- It donates ammonia for biosynthesis or excretion. (correct)
- It only accepts amino groups for energy production.
Which amino acid is directly converted to pyruvate through deamination?
Which amino acid is directly converted to pyruvate through deamination?
- Aspartate
- Glutamine
- Alanine (correct)
- Glutamate
Which of the following is not a key amino acid in nitrogen metabolism?
Which of the following is not a key amino acid in nitrogen metabolism?
- Glutamate
- Alanine
- Aspartate
- Phenylalanine (correct)
During the Glucose-Alanine Cycle, which process occurs in the liver?
During the Glucose-Alanine Cycle, which process occurs in the liver?
What is formed after the removal of the amino group from aspartate?
What is formed after the removal of the amino group from aspartate?
Which mechanism involves the transfer of an amino group to form a different amino acid?
Which mechanism involves the transfer of an amino group to form a different amino acid?
Which statement correctly describes the urea cycle's overall function?
Which statement correctly describes the urea cycle's overall function?
What occurs to the carbon skeleton of an amino acid after deamination?
What occurs to the carbon skeleton of an amino acid after deamination?
Which term refers to the process of removing the amino group from an amino acid?
Which term refers to the process of removing the amino group from an amino acid?
What is the primary purpose of the urea cycle?
What is the primary purpose of the urea cycle?
Which amino acid plays a crucial role in the glucose-alanine cycle?
Which amino acid plays a crucial role in the glucose-alanine cycle?
During transamination, which molecule typically accepts the amino group?
During transamination, which molecule typically accepts the amino group?
Which of the following amino acids is classified as ketogenic?
Which of the following amino acids is classified as ketogenic?
What is the role of pyridoxine (B6) in amino acid metabolism?
What is the role of pyridoxine (B6) in amino acid metabolism?
In the urea cycle, which molecule combines with ammonia to begin the cycle?
In the urea cycle, which molecule combines with ammonia to begin the cycle?
What is the end product of the urea cycle?
What is the end product of the urea cycle?
Which of the following is NOT a function of amino acids in the body?
Which of the following is NOT a function of amino acids in the body?
Which pathway connects the breakdown of amino acids to the central metabolism of the TCA cycle?
Which pathway connects the breakdown of amino acids to the central metabolism of the TCA cycle?
What is the primary role of glutamate dehydrogenase in amino acid metabolism?
What is the primary role of glutamate dehydrogenase in amino acid metabolism?
What is the consequence of increased serum ammonia in the body?
What is the consequence of increased serum ammonia in the body?
How are carbon skeletons from amino acid catabolism utilized in metabolism?
How are carbon skeletons from amino acid catabolism utilized in metabolism?
What role does the urea cycle play in the body?
What role does the urea cycle play in the body?
Which amino acid is notable for not requiring the transfer of its amino group during deamination?
Which amino acid is notable for not requiring the transfer of its amino group during deamination?
What is the primary fate of excess dietary protein in the body?
What is the primary fate of excess dietary protein in the body?
What is the charge of amino groups at physiological pH?
What is the charge of amino groups at physiological pH?
Which amino acid classification is based on the metabolic fate of their carbon backbone?
Which amino acid classification is based on the metabolic fate of their carbon backbone?
What results from deamination of an amino acid?
What results from deamination of an amino acid?
Which of the following best describes hyperammonaemia?
Which of the following best describes hyperammonaemia?
Which amino acid is notably involved in the glucose-alanine cycle?
Which amino acid is notably involved in the glucose-alanine cycle?
How are glucogenic amino acids metabolically significant?
How are glucogenic amino acids metabolically significant?
What is the consequence of cleaving the amino group from an amino acid?
What is the consequence of cleaving the amino group from an amino acid?
Which process is critical for detoxifying ammonia in the body?
Which process is critical for detoxifying ammonia in the body?
What distinguishes essential amino acids from non-essential amino acids?
What distinguishes essential amino acids from non-essential amino acids?
Which enzyme is primarily responsible for the oxidative deamination of amino acids in the liver?
Which enzyme is primarily responsible for the oxidative deamination of amino acids in the liver?
Which of the following describes the process of transamination?
Which of the following describes the process of transamination?
What is the major end product of amino acid deamination in the liver?
What is the major end product of amino acid deamination in the liver?
What important role does alanine play in the glucose-alanine cycle?
What important role does alanine play in the glucose-alanine cycle?
Which amino acid is primarily produced through transamination from pyruvate?
Which amino acid is primarily produced through transamination from pyruvate?
Which of the following amino acids can be classified as a branched-chain amino acid?
Which of the following amino acids can be classified as a branched-chain amino acid?
In the context of the urea cycle, what is the immediate precursor for the synthesis of urea?
In the context of the urea cycle, what is the immediate precursor for the synthesis of urea?
Which amino acid is crucial for nitrogen transport from the muscles to the liver?
Which amino acid is crucial for nitrogen transport from the muscles to the liver?
What is the main metabolic fate of the carbon skeleton derived from deaminated amino acids?
What is the main metabolic fate of the carbon skeleton derived from deaminated amino acids?
In human metabolism, which of the following amino acids is classified as non-essential?
In human metabolism, which of the following amino acids is classified as non-essential?
Flashcards
Glucose-Alanine Cycle
Glucose-Alanine Cycle
A cycle transporting excess nitrogen from muscle to liver, converting it to glucose for export back to muscles.
Deamination
Deamination
The removal of an amino group from an amino acid, generating a carbon skeleton and ammonium.
Alanine
Alanine
An amino acid that transports nitrogen to the liver in the Glucose-Alanine cycle.
Glutamate
Glutamate
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Glutamine
Glutamine
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Pyruvate
Pyruvate
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Carbon skeleton
Carbon skeleton
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Four Key Amino Acids (in Nitrogen Metabolism)
Four Key Amino Acids (in Nitrogen Metabolism)
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Amino Acid Structure
Amino Acid Structure
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Amino Acid Roles
Amino Acid Roles
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Essential vs. Non-essential Amino Acids
Essential vs. Non-essential Amino Acids
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Glucogenic/Ketogenic Amino Acids
Glucogenic/Ketogenic Amino Acids
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Amino Acid Biosynthesis
Amino Acid Biosynthesis
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Amino Acid Metabolism & Central Metabolism
Amino Acid Metabolism & Central Metabolism
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Amino Acid Degradation
Amino Acid Degradation
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Nitrogen Removal
Nitrogen Removal
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Urea Cycle Role
Urea Cycle Role
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Pyridoxine (B6)
Pyridoxine (B6)
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Essential Amino Acids
Essential Amino Acids
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Non-Essential Amino Acids
Non-Essential Amino Acids
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Glucogenic Amino Acids
Glucogenic Amino Acids
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Ketogenic Amino Acids
Ketogenic Amino Acids
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Amino Acid Deamination
Amino Acid Deamination
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Urea Cycle
Urea Cycle
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Amino Acid Metabolism
Amino Acid Metabolism
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TCA Cycle
TCA Cycle
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Gluconeogenesis
Gluconeogenesis
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Aminotransferases
Aminotransferases
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What is the role of Glutamate Dehydrogenase?
What is the role of Glutamate Dehydrogenase?
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What happens to the ammonia produced by Deamination?
What happens to the ammonia produced by Deamination?
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What does hyperammonaemia mean?
What does hyperammonaemia mean?
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How does excess ammonia harm the body?
How does excess ammonia harm the body?
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What is the function of the Urea Cycle?
What is the function of the Urea Cycle?
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Excess dietary protein
Excess dietary protein
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What happens to excess amino acids?
What happens to excess amino acids?
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R group importance
R group importance
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Amino acid charges
Amino acid charges
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Carbon skeleton in metabolism
Carbon skeleton in metabolism
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Ammonia toxicity
Ammonia toxicity
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Why classify amino acids?
Why classify amino acids?
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Study Notes
Amino Acid Metabolism & the Urea Cycle
- Amino acids have unique chemical properties, consisting of a carbon skeleton plus an amine group (-NH2).
- Amino acids play many roles in the body, including building blocks for proteins, precursors for other biologically important molecules, and fuel molecules.
- Dietary intake and synthesis provide amino acids.
- Excess amino acids are converted to fat and used for the body's needs.
- Amino acids are involved in numerous pathways, tissues, and organelles.
- Only the highlights of amino acid metabolism are discussed.
Classification of Amino Acids
- Amino acids can be classified based on physical-chemical properties, dietary needs (essential/nonessential), and metabolic fate of their carbon backbones (gluconeogenic/ketogenic).
- Glucogenic amino acids can be converted to glucose.
- Ketogenic amino acids are broken down for fat synthesis or ketosis.
- Essential amino acids cannot be synthesised by the body.
- Non-essential amino acids can be synthesised by the body.
Amino Acid Biosynthesis
- Humans require essential amino acids from their diet to synthesize non-essential amino acids.
- Two basic components are needed (carbon skeleton + amine donor).
- Amino acids can be derived from various metabolic pathways.
- Essential amino acids are used to synthesize proteins, neurotransmitters, hormones, and haemoglobin.
Metabolic Fate of Dietary & Intracellular Protein
- Cells can remodel amino acids, but most amino acid metabolism takes place in the liver.
- Deamination removes the amino group, and the carbon skeleton is recycled.
- Toxic ammonia is converted to urea in the liver and excreted in urine.
Catabolism of Amino Acids
- Most amino acids undergo deamination in the liver.
- Deamination involves enzymes like aminotransferases and glutamate dehydrogenase.
- Some amino acids are deaminated in skeletal muscle, then transported to the liver for further processing.
Glutamate & Alanine as Nitrogen Transporters
- Glutamate and alanine are major transporters for amino groups between tissues and the liver.
- High levels of these amino acids are present in blood.
Urea Cycle
- High levels of ammonia are toxic.
- The liver and kidneys work together to manage ammonia levels.
- The urea cycle combines two amino groups into a urea molecule.
- Urea is subsequently transported to the kidneys for excretion in urine.
Urea Cycle and TCA Cycle
- The urea and TCA cycles overlap.
- Fumarate from the urea cycle is converted into malate and then into oxaloacetate, an intermediate in the TCA cycle.
- Oxaloacetate is subsequently used to produce aspartate, which enters the urea cycle.
Regulation of the Urea Cycle
- The rate of the urea cycle is regulated through a feed-forward mechanism that responds to ammonia levels.
- Dietary intake of protein affects the urea cycle.
- Regulation occurs at the beginning of the pathway (carbamoyl phosphate synthesis).
Urea Cycle Disorders
- Genetic defects in urea cycle enzymes result in inherited disorders.
- Symptoms usually appear during infancy or early childhood.
- Symptoms associated with urea cycle disorders may include lethargy, seizures, vomiting, and even death in untreated cases.
Clinical Measurement of Urea
- Urea is a significant nitrogen waste product in the body.
- It's synthesized in the liver and majorly cleared by the kidneys.
- Clinically, urea measurements can help track kidney function and detect metabolic or liver disease.
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