Amino Acid Metabolism & Urea Cycle

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Questions and Answers

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?

  • Aspartate
  • Glutamine
  • Alanine (correct)
  • Glutamate

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?

<p>Conversion of alanine into glucose. (C)</p> Signup and view all the answers

What is formed after the removal of the amino group from aspartate?

<p>Oxaloacetate (A)</p> Signup and view all the answers

Which mechanism involves the transfer of an amino group to form a different amino acid?

<p>Transamination (D)</p> Signup and view all the answers

Which statement correctly describes the urea cycle's overall function?

<p>It removes excess nitrogen by forming urea. (A)</p> Signup and view all the answers

What occurs to the carbon skeleton of an amino acid after deamination?

<p>It enters the TCA cycle as an intermediate. (C)</p> Signup and view all the answers

Which term refers to the process of removing the amino group from an amino acid?

<p>Deamination (A)</p> Signup and view all the answers

What is the primary purpose of the urea cycle?

<p>To convert ammonia into urea for excretion (C)</p> Signup and view all the answers

Which amino acid plays a crucial role in the glucose-alanine cycle?

<p>Alanine (B)</p> Signup and view all the answers

During transamination, which molecule typically accepts the amino group?

<p>Glutamate (D)</p> Signup and view all the answers

Which of the following amino acids is classified as ketogenic?

<p>Leucine (D)</p> Signup and view all the answers

What is the role of pyridoxine (B6) in amino acid metabolism?

<p>It acts as a coenzyme in transamination reactions (C)</p> Signup and view all the answers

In the urea cycle, which molecule combines with ammonia to begin the cycle?

<p>Ornithine (B)</p> Signup and view all the answers

What is the end product of the urea cycle?

<p>Urea (D)</p> Signup and view all the answers

Which of the following is NOT a function of amino acids in the body?

<p>Energy storage (B)</p> Signup and view all the answers

Which pathway connects the breakdown of amino acids to the central metabolism of the TCA cycle?

<p>Amino acid degradation (D)</p> Signup and view all the answers

What is the primary role of glutamate dehydrogenase in amino acid metabolism?

<p>It promotes the oxidative deamination of glutamate to remove ammonia. (C)</p> Signup and view all the answers

What is the consequence of increased serum ammonia in the body?

<p>Activation of NMDA receptors and excess glutamate levels. (A)</p> Signup and view all the answers

How are carbon skeletons from amino acid catabolism utilized in metabolism?

<p>They can enter the TCA cycle or glycolysis for energy production. (A)</p> Signup and view all the answers

What role does the urea cycle play in the body?

<p>It minimizes the risks associated with excess ammonia in circulation. (B)</p> Signup and view all the answers

Which amino acid is notable for not requiring the transfer of its amino group during deamination?

<p>Glutamate (A)</p> Signup and view all the answers

What is the primary fate of excess dietary protein in the body?

<p>It undergoes deamination and is converted to fatty acids. (A)</p> Signup and view all the answers

What is the charge of amino groups at physiological pH?

<p>Positively charged (NH3+) (C)</p> Signup and view all the answers

Which amino acid classification is based on the metabolic fate of their carbon backbone?

<p>Glucogenic/ketogenic (C)</p> Signup and view all the answers

What results from deamination of an amino acid?

<p>Release of nitrogenous waste and an alpha-keto acid. (C)</p> Signup and view all the answers

Which of the following best describes hyperammonaemia?

<p>Accumulation of free ammonia in the body. (C)</p> Signup and view all the answers

Which amino acid is notably involved in the glucose-alanine cycle?

<p>Alanine (D)</p> Signup and view all the answers

How are glucogenic amino acids metabolically significant?

<p>They can be converted to glucose through gluconeogenesis. (A)</p> Signup and view all the answers

What is the consequence of cleaving the amino group from an amino acid?

<p>It forms a carbon skeleton that can be recycled. (C)</p> Signup and view all the answers

Which process is critical for detoxifying ammonia in the body?

<p>Urea cycle (C)</p> Signup and view all the answers

What distinguishes essential amino acids from non-essential amino acids?

<p>Essential amino acids cannot be synthesized by the body. (B)</p> Signup and view all the answers

Which enzyme is primarily responsible for the oxidative deamination of amino acids in the liver?

<p>Glutamate dehydrogenase (D)</p> Signup and view all the answers

Which of the following describes the process of transamination?

<p>Transfer of an amine group to a keto acid (C)</p> Signup and view all the answers

What is the major end product of amino acid deamination in the liver?

<p>Urea (C)</p> Signup and view all the answers

What important role does alanine play in the glucose-alanine cycle?

<p>It transports amine groups from muscle to liver (A)</p> Signup and view all the answers

Which amino acid is primarily produced through transamination from pyruvate?

<p>Alanine (A)</p> Signup and view all the answers

Which of the following amino acids can be classified as a branched-chain amino acid?

<p>Isoleucine (B)</p> Signup and view all the answers

In the context of the urea cycle, what is the immediate precursor for the synthesis of urea?

<p>Carbamoyl phosphate (A)</p> Signup and view all the answers

Which amino acid is crucial for nitrogen transport from the muscles to the liver?

<p>Alanine (A)</p> Signup and view all the answers

What is the main metabolic fate of the carbon skeleton derived from deaminated amino acids?

<p>Conversion to glucose or ketone bodies (D)</p> Signup and view all the answers

In human metabolism, which of the following amino acids is classified as non-essential?

<p>Glycine (C)</p> Signup and view all the answers

Flashcards

Glucose-Alanine Cycle

A cycle transporting excess nitrogen from muscle to liver, converting it to glucose for export back to muscles.

Deamination

The removal of an amino group from an amino acid, generating a carbon skeleton and ammonium.

Alanine

An amino acid that transports nitrogen to the liver in the Glucose-Alanine cycle.

Glutamate

Amino acid that acts as an ammonia acceptor (in AA degradation) and donor (for biosynthesis/excretion).

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Glutamine

An amino acid, a key transporter of amino groups between tissues and the liver, and a higher level in blood versus other amino acids.

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Pyruvate

Precursor for gluconeogenesis formed during Alanine deamination.

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Carbon skeleton

The part of an amino acid remaining after deamination.

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Four Key Amino Acids (in Nitrogen Metabolism)

Alanine, Aspartate, Glutamate, and Glutamine are key players in transporting/removing nitrogen.

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Amino Acid Structure

Amino acids are small molecules with a carbon skeleton and an amine group (-NH2).

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Amino Acid Roles

Amino acids have multiple roles, including building proteins, creating other molecules, and acting as fuel.

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Essential vs. Non-essential Amino Acids

Essential amino acids are obtained through diet, while non-essential amino acids are made by the body.

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Glucogenic/Ketogenic Amino Acids

Amino acids that can be converted to glucose or ketone bodies.

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Amino Acid Biosynthesis

The process of creating amino acids within the body.

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Amino Acid Metabolism & Central Metabolism

Amino acid metabolism connects with the main metabolic pathways, like the TCA cycle.

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Amino Acid Degradation

The breakdown of amino acids.

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Nitrogen Removal

The process of removing nitrogen from amino acids to form carbon skeletons.

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Urea Cycle Role

The urea cycle converts ammonia into urea to remove nitrogen.

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Pyridoxine (B6)

A B vitamin important in amino acid metabolism.

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Essential Amino Acids

Amino acids that the body cannot synthesize and must be obtained from the diet.

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Non-Essential Amino Acids

Amino acids that the body can synthesize from other compounds.

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Glucogenic Amino Acids

Amino acids whose carbon skeletons can be converted to glucose.

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Ketogenic Amino Acids

Amino acids whose carbon skeletons can be converted into ketone bodies.

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Amino Acid Deamination

The removal of an amino group from an amino acid.

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Urea Cycle

A process in the liver that converts toxic ammonia to less harmful urea, which is excreted.

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Amino Acid Metabolism

The breakdown and synthesis of amino acids in the body.

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TCA Cycle

A metabolic pathway where amino acid carbon skeletons can enter for energy production.

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Gluconeogenesis

The production of glucose from non-carbohydrate sources, such as amino acids.

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Aminotransferases

Enzymes that catalyze the transfer of an amino group from one molecule to another.

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What is the role of Glutamate Dehydrogenase?

Glutamate Dehydrogenase is an enzyme involved in oxidative deamination of glutamate, removing its amino group and producing α-ketoglutarate, NADH, H+ and ammonium. This process is crucial for ammonia metabolism.

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What happens to the ammonia produced by Deamination?

The ammonium produced during deamination is used to form urea, which is a less toxic form of nitrogen that can be excreted by the body.

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What does hyperammonaemia mean?

Hyperammonaemia refers to an elevated ammonia level in the blood, a potentially dangerous condition as ammonia readily crosses the blood-brain barrier by diffusion.

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How does excess ammonia harm the body?

Excess ammonia can lead to several toxic effects, including: increased levels of glutamate (excitotoxin), activation of NMDA receptors, elevated glutamine, depletion of ATP, and brain swelling.

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What is the function of the Urea Cycle?

The urea cycle is a metabolic process that minimizes the risk of excess ammonia in the body by converting ammonia into urea for excretion.

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Excess dietary protein

When we eat more protein than our body needs, it's not stored as protein. Instead, it's broken down into amino acids and used for energy or converted to fat.

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What happens to excess amino acids?

Excess amino acids are broken down into their carbon skeletons and amino groups. The carbon skeletons are used for energy or stored as fat, while the amino groups are converted to urea for excretion.

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R group importance

The R group, or side chain, gives each amino acid its unique properties. This variation allows for a wide range of protein structures and functions.

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Amino acid charges

At physiological pH, amino groups are positively charged (NH3+) and carboxyl groups are negatively charged (COO-).

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Carbon skeleton in metabolism

Metabolically, amino acids are considered as a carbon skeleton (alpha keto acid) and an amino group. The carbon skeleton can be recycled for energy or biosynthesis.

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Ammonia toxicity

Free ammonia is toxic and can cause brain swelling, coma, and death. Careful handling of the amino groups is important during amino acid metabolism.

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Why classify amino acids?

Amino acids can be classified by their side chain properties, metabolic fate (glucogenic/ketogenic), and dietary availability (essential/non-essential). This classification helps understand their specific roles in the body.

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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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