Glycogen Formation and Breakdown

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Questions and Answers

Why can the liver provide glucose to other organs?

  • Because it contains more glycogen than muscle
  • Because it converts G6P into G1P
  • Because it produces glucose through gluconeogenesis
  • Because it can release glucose out of the cell (correct)

What is the reason that glucose is trapped in muscle cells?

  • Muscle cells do not convert glucose into G1P
  • Muscle cells can only phosphorylate glucose to G6P (correct)
  • Muscle cells use glucose solely for energy production
  • Muscle cells lack the enzymes to secrete glucose

What is the product formed from the phosphorylation of glucose?

  • Glucose-6-phosphate (G6P) (correct)
  • Limit dextrin
  • Glucose-1-phosphate (G1P)
  • Glycogen

What limits further cleavage of glycogen when it becomes limit dextrin?

<p>The inability of glycogen phosphorylase to recognize residues (A)</p> Signup and view all the answers

Which coenzyme is involved in the conversion of vitamin B6 during this process?

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

What is the primary function of oxidative deamination in amino acid metabolism?

<p>To convert an amino acid to a keto acid while releasing ammonium ion (A)</p> Signup and view all the answers

Which coenzyme is involved in the action of glutamate dehydrogenase during oxidative deamination?

<p>NAD (A), NADP (C)</p> Signup and view all the answers

What role does fumarate play in the context of the Krebs cycle after amino acid breakdown?

<p>It reenters the Krebs cycle. (D)</p> Signup and view all the answers

Where does oxidative deamination primarily occur in the body?

<p>In the mitochondria of the liver (D)</p> Signup and view all the answers

Which of the following amino acids can return to the TCA cycle through oxaloacetate?

<p>Arginine (C), Aspartate (D)</p> Signup and view all the answers

What kind of amino acids can be converted back to succinyl CoA?

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

How does glutamate dehydrogenase differ from other enzymes?

<p>It can utilize multiple types of coenzymes. (A)</p> Signup and view all the answers

What is formed when ammonium ion combines with water molecules during oxidative deamination?

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

What role does the niacin group play in metabolism?

<p>It can become a coenzyme. (D)</p> Signup and view all the answers

What is the lifespan of red blood cells (RBC)?

<p>80 to 120 days (B)</p> Signup and view all the answers

What happens to damaged red blood cells?

<p>They are consumed by macrophages. (B)</p> Signup and view all the answers

What component of hemoglobin is processed into bilirubin?

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

Where does bilirubin go for conjugation and processing?

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

What is released from hemoglobin during its catabolism?

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

What process utilizes alpha-ketoglutarate aside from the Krebs cycle?

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

What happens to alpha-ketoglutarate after its generation?

<p>It is reused in metabolic pathways. (D)</p> Signup and view all the answers

What is the storage form of iron in the body?

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

What substance is produced from the breakdown of the heme group?

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

Which enzyme is responsible for converting bilirubin to its conjugated form?

<p>UDP glucuronyl transferase (A)</p> Signup and view all the answers

What do stercobilin and urobilinogen turn into in the body?

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

Which of the following is a product produced from the gastrointestinal processing of conjugated bilirubin?

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

Which organ primarily processes the unconjugated bilirubin created from the heme group?

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

What process converts damaged red blood cells into bilirubin?

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

What is the main role of probiotics in the gastrointestinal system concerning bilirubin?

<p>Process conjugated bilirubin (C)</p> Signup and view all the answers

What is the role of the gallbladder during fasting?

<p>It releases stored bile to aid in lipid digestion. (B)</p> Signup and view all the answers

What happens to the TCA cycle during a state of fasting?

<p>It slows down due to lack of glucose provision. (C)</p> Signup and view all the answers

Which of the following is a byproduct formed from beta-oxidation during fasting?

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

Where do ketone bodies primarily form in the body?

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

What is the first ketone body produced during ketogenesis?

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

Which of the following statements is true regarding lacteals?

<p>They absorb lipids first in the small intestine. (B)</p> Signup and view all the answers

What catalyzes the production of β-Hydroxybutyrate from acetoacetate?

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

How are lipids transported through the bloodstream after absorption?

<p>As chylomicrons and other lipoproteins. (A)</p> Signup and view all the answers

What is formed through the condensation of two acetyl CoA molecules?

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

Which substance will not result in ketone body formation?

<p>Sufficient glucose levels (B)</p> Signup and view all the answers

What is the primary energy source produced during fasting?

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

What triggers the production of ketone bodies in the liver?

<p>Build-up of acetyl CoA (D)</p> Signup and view all the answers

What occurs to excess Acetyl CoA that is not used in the TCA cycle?

<p>Converted to ketone bodies. (C)</p> Signup and view all the answers

What does lipolysis lead to during the fasting state?

<p>Release of fatty acids and glycerol. (D)</p> Signup and view all the answers

What is the primary role of specific transporters in amino acid metabolism?

<p>To transport individual amino acids into cells (C)</p> Signup and view all the answers

Which of the following accurately describes the digestion of proteins?

<p>Involves hydrochloric acid and pepsin in the stomach (A)</p> Signup and view all the answers

What happens to excess amino acids that are not used by the body?

<p>They are catabolized for energy (C)</p> Signup and view all the answers

Which process does NOT occur during protein catabolism?

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

What is the primary function of hydrochloric acid in protein digestion?

<p>To hydrolyze peptide bonds (D)</p> Signup and view all the answers

Which statement about amino acids is accurate?

<p>They cannot be stored and must be catabolized for energy (D)</p> Signup and view all the answers

What triggers the release of zymogens in the small intestine?

<p>The arrival of large polypeptides (A)</p> Signup and view all the answers

What is a key purpose of the urea cycle?

<p>To excrete excess nitrogen from amino acid breakdown (B)</p> Signup and view all the answers

Which enzyme is primarily responsible for hydrolyzing peptide bonds during digestion?

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

During amino acid catabolism, which group is removed first?

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

What is the approximate pH of hydrochloric acid in the stomach?

<p>Acidic (1.5 - 2.0) (A)</p> Signup and view all the answers

In what part of the body does the catabolism of amino acids primarily occur?

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

After amino acid catabolism, what is the fate of the carbon skeleton?

<p>Used for energy production (A)</p> Signup and view all the answers

Flashcards

Glycogen from Liver

Liver glycogen can release glucose into other organs.

Muscle Glycogen

Muscle glycogen is used only by the muscle itself; it cannot be shared.

G6P in Muscle

Glucose-6-Phosphate (G6P) is the form of glucose found in muscle cells.

Glycogen Phosphorylase

An enzyme that breaks down glycogen into glucose.

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Limit Dextrin

The remaining 4 units of glucose after glycogen phosphorylase acts on the glycogen chain.

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Ketone Bodies

Byproducts formed from the beta-oxidation of fatty acids during fasting.

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Ketogenesis

The process of synthesizing ketone bodies from acetyl CoA.

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Acetoacetate

The first ketone body produced in ketogenesis.

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β-Hydroxybutyrate

A ketone body produced from the reduction of acetoacetate.

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Acetone

A ketone body produced in the bloodstream.

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Beta-oxidation

The breakdown of fatty acids to produce acetyl CoA.

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Acetyl CoA

A molecule important in both carbohydrate and fat metabolism.

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Fasting

A period without food intake.

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Common bile duct

A duct that carries bile from the liver and gallbladder to the small intestine.

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Pancreatic lipases

Enzymes produced by the pancreas that aid in fat digestion.

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Small intestine

Part of the digestive system where most nutrient absorption takes place.

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Lacteals

Specialized lymphatic vessels that absorb lipids in the small intestine.

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Chylomicrons

Packages that transport lipids from the small intestine to the bloodstream.

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Liver mitochondria

Location where ketogenesis occurs.

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Hepatocytes

Liver cells.

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Oxidative Deamination

The process of removing an amine group (NH2) from an amino acid, converting it to a keto acid and releasing ammonium ions (NH4+).

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Glutamate Deamination

Oxidative deamination of glutamate, a common amino acid, produces alpha-ketoglutarate and ammonium ions. This process is essential for nitrogen removal in the body.

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Where does Oxidative Deamination Occur?

Oxidative deamination mainly takes place within the mitochondria of liver cells.

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Glutamate Dehydrogenase

The enzyme responsible for catalyzing oxidative deamination of glutamate. It can utilize either NAD or NADP as cofactors.

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How Does Urea Form?

Ammonium ions released from oxidative deamination are converted to urea through a series of reactions. Fumarate, a product of the Krebs cycle, interacts with aspartate, leading to the formation of arginine, which eventually breaks down to urea.

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Reversing the Krebs Cycle for Urea Removal

Some amino acids are broken down into intermediates that can re-enter the Krebs cycle, aiding in the removal of urea and maintaining metabolic balance.

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Amino Acid Re-entry into the Krebs Cycle

Examples include arginine and aspartate entering through oxaloacetate, isoleucine, methionine, and valine entering through succinyl CoA, and isoleucine, leucine, and tryptophan entering through acetyl CoA.

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Why is Oxidative Deamination Important?

Oxidative deamination is a critical process in nitrogen removal, as it removes ammonia from the body. This is vital for preventing toxicity and maintaining proper cell function.

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Hemoglobin Catabolism

The breakdown of hemoglobin, the protein responsible for carrying oxygen in red blood cells.

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Globin Part

The protein component of hemoglobin, which is broken down into amino acids.

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Heme Part

The non-protein part of hemoglobin containing iron, which is converted into bilirubin.

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Bilirubin

A yellow pigment produced from the breakdown of heme, transported to the liver for processing.

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Liver Processing of Bilirubin

The liver conjugates bilirubin with glucuronic acid, making it water-soluble and easier to excrete in bile.

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Alpha Ketoglutarate

A molecule produced in the Krebs cycle that can be used in other biochemical processes.

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Transamination

A chemical reaction that transfers an amino group from one molecule to another.

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Urea Cycle

A metabolic pathway that converts ammonia, a toxic waste product, into urea for excretion.

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Protein Turnover

The continuous process of protein breakdown and synthesis within the body, crucial for maintaining a balance of amino acids for various functions.

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Stages of Protein Turnover

There are two main stages: removal of the amino group (deamination) and degradation of the carbon skeleton.

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Why can't we store amino acids?

Amino acids are not stored in the body, unlike carbohydrates and fats. They are either used for protein synthesis or broken down for energy.

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Amino Acid Transport

Individual amino acids are transported into cells using specific transporters, with one transporter for each type of amino acid.

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Amino Acid Reuse

Amino acids can be reused for protein synthesis within the body, meaning they're not always broken down.

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What happens to excess amino acids?

Excess amino acids, not used for protein synthesis, are catabolized (broken down) for energy production in the liver.

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Protein Digestion in Stomach

Protein digestion begins in the stomach with the action of hydrochloric acid (HCl) and pepsin.

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Hydrochloric Acid's Role in Digestion

HCl is crucial for protein digestion, breaking down proteins and creating a very acidic environment (pH 1.5 to 2).

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Pepsin and Protein Hydrolysis

Pepsin, a protease enzyme, helps break down peptide bonds within proteins in the stomach.

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Large Polypeptides in the Small Intestine

By the time digested proteins reach the small intestine, they are in the form of large polypeptides.

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Release of Zymogens from Pancreas

The presence of large polypeptides in the small intestine triggers the release of inactive enzymes called zymogens from the pancreas.

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Iron Storage

Ferritin is the primary storage form of iron within the body.

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Heme Breakdown

When red blood cells break down, macrophages release the heme group, which is further processed to produce bilirubin.

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Bilirubin Formation

Heme is converted to bilirubin by heme oxygenase and bilirubin reductase.

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Conjugated Bilirubin

In the liver, bilirubin is conjugated with glucuronic acid, making it water-soluble.

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Stercobilin

Conjugated bilirubin is processed by intestinal bacteria to form stercobilin, which is excreted in feces.

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Urobilinogen

Conjugated bilirubin is also processed into urobilinogen, which is excreted in urine.

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Red Blood Cell Breakdown

Damaged red blood cells are broken down by macrophages, releasing heme and other components.

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Iron Release

When heme is broken down, iron is released and stored in ferritin.

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Study Notes

Glycogen Formation and Breakdown

  • Glycogen is the storage form of carbohydrates in animals
  • Primarily found in muscle and liver tissues
  • Made up of alpha-d glucose units

Glycogen Synthesis (Glycogenesis)

  • Insulin stimulates glycogen synthase and glucokinase
  • Main enzyme during fed state, enabling glucose entry into cells for storage or glycolysis
  • Glucagon and epinephrine inhibit glycogen synthase, preventing glycogen storage during fasting/starving
  • Crucial for storing excess glucose

Glycogen Breakdown (Glycogenolysis)

  • Glycogenolysis is the opposite of glycogenesis
  • Important for releasing glucose during fasting/starving
  • Process influenced by hormones to release stored glucose
  • Insulin inhibits while glucagon and epinephrine stimulate glycogenolysis

Glycogen Isomerization

  • Enzyme: Phosphoglucomutase
  • Converts glucose-1-phosphate to glucose-6-phosphate

Glycogen Activation

  • UDP-glucose pyrophosphorylase catalyzes addition of UTP to glucose-1-phosphate, creating UDP-glucose
  • Important for glucose attachment to the glycogen chain

Glycogen Branching

  • Enzyme: Amylo (α1→4) → α(1→6) transglucosidase
  • Forms α(1→6) bonds, creating branching points on the glycogen chain

Glycogen Transfer

  • Enzyme: Glucan transferase
  • Transfers 3-8 glucosyl residues from the outer chain to the core chain to create branches

Glycogen Debranching

  • Enzyme: Amylo α(1→6) glucosidase
  • Cleaves α(1→6) bonds, releasing free glucose

Glycogenolysis - Summary

  • Cleavage of α(1→4) bonds → yields glucose-1-phosphate
  • Continue until the limit dextrin (4 glucosyl units)
  • Glucose-1-phosphate is converted to glucose-6-phosphate
  • Glucose-6-phosphatase (only in liver) converts glucose-6-phosphate to free glucose for release into bloodstream; muscle only produces glucose-6-phosphate

Glycogenolysis - Liver vs. Muscle

  • Liver glycogenolysis produces free glucose for release into the blood
  • Muscle glycogenolysis produces glucose-6-phosphate which remains in the muscle, only to be later used during glycolysis

Other Metabolic Pathways

  • Muscle glycogen → G6P → glycolysis; liver glycogen → G6P → glucose
  • Glucose-6-phosphate → free glucose (liver only)
  • Glucagon and epinephrine stimulate glycogen phosphorylase; insulin inhibits

Other Important Notes

  • Mutase: shifts phosphate groups
  • Coenzyme: Vitamin B6 (Pyridoxal phosphate)
  • G6P in muscle can't be released to the bloodstream as glycogen is stored only for the muscle
  • G6P in liver converts glucose-6-phosphate to glucose for release in the blood stream

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