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Questions and Answers
Which amino acid is linked to heart disease?
Which amino acid is linked to heart disease?
What is the primary process by which proteins are broken down into amino acids?
What is the primary process by which proteins are broken down into amino acids?
In the synthesis of amino acids, what process is used to form amino groups from metabolic intermediates?
In the synthesis of amino acids, what process is used to form amino groups from metabolic intermediates?
How are glucogenic amino acids primarily metabolized?
How are glucogenic amino acids primarily metabolized?
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What is the result of the urea cycle in amino acid metabolism?
What is the result of the urea cycle in amino acid metabolism?
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Which amino acids are considered essential?
Which amino acids are considered essential?
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What is the precursor for the synthesis of serine?
What is the precursor for the synthesis of serine?
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Which amino acid becomes essential if there is restricted dietary availability of phenylalanine?
Which amino acid becomes essential if there is restricted dietary availability of phenylalanine?
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Which of the following amino acids is not formed from metabolic intermediates?
Which of the following amino acids is not formed from metabolic intermediates?
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How is cysteine synthesized?
How is cysteine synthesized?
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What role does dihydrobiopterin reductase play in tyrosine synthesis?
What role does dihydrobiopterin reductase play in tyrosine synthesis?
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Which two amino acids are considered semi-essential?
Which two amino acids are considered semi-essential?
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Which metabolic intermediate is not associated with the synthesis of asparagine?
Which metabolic intermediate is not associated with the synthesis of asparagine?
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What role do transaminase enzymes play in the body?
What role do transaminase enzymes play in the body?
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Which of the following correctly describes the role of amino acids in gluconeogenesis?
Which of the following correctly describes the role of amino acids in gluconeogenesis?
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What is the primary function of essential amino acids?
What is the primary function of essential amino acids?
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In which process are amino acids primarily eliminated from the body?
In which process are amino acids primarily eliminated from the body?
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What is a consequence of OTC Deficiency?
What is a consequence of OTC Deficiency?
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Which component of amino acids determines their identity?
Which component of amino acids determines their identity?
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Which of the following is NOT a role of amino acids in the body?
Which of the following is NOT a role of amino acids in the body?
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What is the approximate total pool of amino acids in the human body?
What is the approximate total pool of amino acids in the human body?
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What role do muscle and liver primarily play in amino acid levels during fasting?
What role do muscle and liver primarily play in amino acid levels during fasting?
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Which enzyme is primarily responsible for transferring amino groups between amino acids?
Which enzyme is primarily responsible for transferring amino groups between amino acids?
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What is the primary consequence of hyperammonaemia?
What is the primary consequence of hyperammonaemia?
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How is ammonia primarily disposed of in the body?
How is ammonia primarily disposed of in the body?
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What is the rate-limiting step in the urea cycle?
What is the rate-limiting step in the urea cycle?
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What is the role of glutamate dehydrogenase in the nitrogen metabolism pathway?
What is the role of glutamate dehydrogenase in the nitrogen metabolism pathway?
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Which amino acid primarily serves as the nitrogen donor in transamination reactions?
Which amino acid primarily serves as the nitrogen donor in transamination reactions?
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What happens to alanine synthesized in muscle during fasting?
What happens to alanine synthesized in muscle during fasting?
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Which of the following statements accurately describes the equilibrium constant of aminotransferases?
Which of the following statements accurately describes the equilibrium constant of aminotransferases?
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What is one of the main symptoms of Ornithine Transcarbamoylase (OTC) deficiency?
What is one of the main symptoms of Ornithine Transcarbamoylase (OTC) deficiency?
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During glutamine transport to the liver, which enzyme converts glutamine back into ammonia and glutamate?
During glutamine transport to the liver, which enzyme converts glutamine back into ammonia and glutamate?
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Which of the following processes involves the generation of glutamate?
Which of the following processes involves the generation of glutamate?
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What is a common treatment for severe cases of OTC deficiency?
What is a common treatment for severe cases of OTC deficiency?
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Which of the following is NOT a source of ammonia in the body?
Which of the following is NOT a source of ammonia in the body?
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Study Notes
Learning Objectives
- Understand the functions of amino acids in bodily processes.
- Distinguish between essential and non-essential amino acids.
- Recognize the role of transaminase enzymes in amino acid metabolism.
- Describe how amino acids serve as substrates in gluconeogenesis, ketogenesis, and energy metabolism.
- Explain ureogenesis and the mechanism of amino nitrogen elimination.
- Examine OTC deficiency as a pathophysiological example.
Amino Acid Structure
- Amino acids consist of an α-carboxyl group, an α-amino group, and a side chain (R-group) that defines identity.
- The general formula: R-CH(COOH)-NH2.
Functions of Amino Acids
- Serve as building blocks for proteins: enzymes, receptors, hormones, and transport proteins.
- Precursor for smaller bioactive compounds:
- Hemes from glycine.
- Nucleic acids (purines and pyrimidines) from aspartate, glycine, and glutamine.
- Hormones like thyroxine.
- Neurotransmitters (dopamine, catecholamines, serotonin, glutamate).
Protein Turnover and Amino Acid Pool
- Average protein turnover includes approximately 12 kg in the body with around 100 g in circulation.
- Amino acid levels are maintained through tissue utilization and release from stores, chiefly in muscle and liver.
Amino Acid Degradation
- Degraded into two categories: glucogenic (precursors to glucose) and ketogenic (precursors to ketone bodies).
- Catabolism involves transamination, where amino groups are transferred, forming glutamate, acting as a universal amino donor.
Transamination
- Transamination reactions predominantly generate glutamate.
- Aminotransferase enzymes facilitate the process, named after the amino donor.
- Glutamate collects amino groups, allowing for amino acid degradation and synthesis.
Glucose-Alanine Cycle
- Alanine, synthesized in muscle via transamination, travels to the liver, where it is converted to glucose and urea.
Glutamate Dehydrogenase
- Converts glutamate to α-ketoglutarate, releasing ammonia.
- Facilitates nitrogen release, providing carbon skeletons for gluconeogenesis.
- Reaction direction is influenced by substrate concentrations and allosteric control (ATP inhibits, ADP activates).
Ammonia
- Neurotoxin; hyperammonaemia leads to slurred speech, blurred vision, tremors, mental confusion, and potential coma.
- Disposal occurs via the urea cycle in the liver.
- Sources of ammonia include transamination, urea breakdown by gut bacteria, and purine/pyrimidine metabolism.
Transport of Nitrogen to Liver
- Glutamine synthetase converts glutamate and ammonia into glutamine for transport to the liver.
- Alanine is converted to pyruvate and glutamate in the liver, contributing to gluconeogenesis.
Urea Cycle
- Urea synthesized in the liver is water-soluble and excreted via the kidneys.
- Processes four substrates (aspartate, NH3, CO2) and five enzymes, with carbamoyl phosphate synthase as the rate-limiting step.
Pathophysiological Example: OTC Deficiency
- OTC deficiency is an X-linked disorder causing hyperammonaemia, presenting with anorexia, irritability, and lethargy.
- Treatments include a low-protein diet, medications for nitrogen excretion, and potential liver transplant.
Amino Acid Classification
- Essential amino acids: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine.
- Semi-essential: arginine, histidine (essential for children).
- Non-essential: alanine, asparagine, aspartate, cysteine, glutamate, glutamine, proline, serine, glycine, tyrosine.
Synthesis of Non-Essential Amino Acids
- Various metabolic intermediates and enzymes facilitate the synthesis of non-essential amino acids from essential ones and other precursors.
Cysteine and Methionine Metabolism
- Cysteine is synthesized from methionine and serine; methionine is necessary for sulfur supply and links to cardiovascular health through homocysteine levels.
Overview of Protein Metabolism
- Proteins undergo proteolysis into amino acids or are synthesized from amino acids.
- Amino acid catabolism can yield substrates for gluconeogenesis or feed into the urea cycle for nitrogen removal.
Recommended Reading
- Lippincott’s Ch. 19 and 20; Meisenberg and Simmons Ch. 26 for deeper understanding of amino acid metabolism and biochemistry.
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Description
Test your knowledge about amino acids and their relation to heart disease. This quiz covers the breakdown of proteins, the urea cycle, essential amino acids, and their metabolism. Challenge yourself and learn more about the crucial role amino acids play in human health.
