Biochemistry and Physiology test 3

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Questions and Answers

Which of the following is an example of a disaccharide?

  • Glucose
  • Galactose
  • Sucrose (correct)
  • Fructose

In what form do monosaccharides exist?

  • Both linear (Fischer projection) and cyclic (Haworth projection) forms (correct)
  • Linear form only
  • Cyclic form only
  • Neither linear nor cyclic forms

What type of ring structure does glucose form?

  • Four-membered ring
  • Six-membered pyranose ring (correct)
  • Three-membered ring
  • Five-membered furanose ring

What is the initial enzyme involved in protein digestion within the stomach?

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

Which pancreatic proteases cleave peptide bonds into smaller peptides in the small intestine?

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

Which of the following enzymes removes terminal amino acids from proteins?

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

What is the process by which free amino acids are absorbed?

<p>Na+-dependent active transport (D)</p> Signup and view all the answers

What is the function of Rumen Undegradable Protein (RUP) in ruminants?

<p>It passes to the small intestine for absorption. (C)</p> Signup and view all the answers

What type of enzymes are primarily relied upon for protein digestion in non-ruminants?

<p>Gastric and pancreatic enzymes (A)</p> Signup and view all the answers

Which of the following is a key component of cell membranes?

<p>Lipids, proteins, and carbohydrates (C)</p> Signup and view all the answers

How are carbohydrates typically associated with the cell membrane?

<p>Attached to proteins (glycoproteins) or lipids (glycolipids) (B)</p> Signup and view all the answers

What is the main difference between passive and active transport across cell membranes?

<p>Active transport requires energy; passive transport does not. (A)</p> Signup and view all the answers

What is the role of aquaporins in membrane transport?

<p>Water movement through the membrane (C)</p> Signup and view all the answers

What type of glycosidic bonds are found in amylose?

<p>α-1,4 glycosidic bonds (A)</p> Signup and view all the answers

Which of the following is a structural component of plants and contains β-1,4 glycosidic bonds?

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

What color change indicates a positive result in the iodine test for starch detection?

<p>Blue-black (D)</p> Signup and view all the answers

What is the net ATP usage in the energy investment phase (reactions 1-5) of glycolysis?

<p>-2 ATP (C)</p> Signup and view all the answers

Which enzyme catalyzes the conversion of glucose to glucose-6-phosphate (G6P) during glycolysis?

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

What is the main reason for lactate production in anaerobic conditions?

<p>To regenerate NAD+ for glycolysis to continue (A)</p> Signup and view all the answers

What are the products of pyruvate conversion to Acetyl-CoA under aerobic conditions?

<p>CO2, NADH, and Acetyl-CoA (B)</p> Signup and view all the answers

Which coenzyme is bound to E1 in the Pyruvate Dehydrogenase Complex (PDC)?

<p>Thiamine Pyrophosphate (TPP) (A)</p> Signup and view all the answers

Which of the following coenzymes is regenerated in the oxidative decarboxylation of pyruvate?

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

What is the first step in the Krebs cycle?

<p>Acetyl-CoA + Oxaloacetate → Citrate (C)</p> Signup and view all the answers

Which reaction in the Krebs cycle produces FADH2?

<p>Succinate → Fumarate (B)</p> Signup and view all the answers

What is the net ATP gain from glycolysis to pyruvate?

<p>2 ATP (B)</p> Signup and view all the answers

During Glycogenolysis, which enzyme removes glucose from the non-reducing ends of glycogen?

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

What type of glycosidic bonds does glycogen synthase form during glycogen synthesis?

<p>α(1→4) glycosidic bonds (B)</p> Signup and view all the answers

What is the main function of NADPH produced in the pentose phosphate pathway?

<p>Fatty acid synthesis and maintaining glutathione in its reduced form (C)</p> Signup and view all the answers

Which enzyme is deficient in Glucose-6-Phosphate Dehydrogenase Deficiency, leading to hemolysis in RBCs?

<p>Glucose-6-Phosphate Dehydrogenase (C)</p> Signup and view all the answers

Which enzyme involved in gluconeogenesis converts pyruvate to oxaloacetate?

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

What is the role of ATP in anabolic reactions?

<p>To provide energy for biosynthesis (A)</p> Signup and view all the answers

In which metabolic processes does substrate-level phosphorylation occur?

<p>Both glycolysis and Krebs cycle (C)</p> Signup and view all the answers

What is the final electron acceptor in oxidative phosphorylation?

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

How many ATP molecules are produced from NADH oxidation during oxidative phosphorylation?

<p>3 ATP (B)</p> Signup and view all the answers

What is the function of the $F_0$ subunit in ATP synthase?

<p>Acts as a proton channel that allows H+ back into the matrix (C)</p> Signup and view all the answers

Which process describes the breakdown of complex molecules to release energy?

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

What is the primary function of the liver in maintaining blood glucose levels?

<p>Storing glucose as glycogen or converting it to lipids (B)</p> Signup and view all the answers

What is the process by which amino acids are converted into keto acids?

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

What is the role of chylomicrons in lipid metabolism?

<p>Transport dietary lipids (A)</p> Signup and view all the answers

Which hormone lowers glucose and fatty acids in plasma?

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

Flashcards

Monosaccharides

Simplest carbohydrates that cannot be hydrolyzed further.

Disaccharides

Carbohydrates composed of two monosaccharide units.

Pepsin

Enzyme in the stomach that hydrolyzes proteins into polypeptides, activated by HCl.

Trypsin & Chymotrypsin

Pancreatic enzymes that cleave peptide bonds into smaller peptides in the small intestine.

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Carboxypeptidase

Enzyme in the small intestine that removes terminal amino acids from peptides.

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Phospholipid Bilayer

Membrane structure composed of hydrophilic heads facing outward and hydrophobic tails facing inward.

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Integral Proteins

Membrane proteins fully embedded in the membrane, aiding in transport.

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Peripheral Proteins

Membrane proteins attached to membrane surfaces, involved in signaling.

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Diffusion

Movement from high to low concentration without energy.

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Facilitated Diffusion

Passive transport using carrier or channel proteins.

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Osmosis

Water movement through a membrane via aquaporins.

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Primary Active Transport

Direct use of ATP for transport (e.g., Sodium-Potassium pump).

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Secondary Active Transport

Uses energy from another molecule's concentration gradient for transport.

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Endocytosis

Engulfing substances into the cell.

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Exocytosis

Releasing substances out of the cell.

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Amylose

Unbranched starch with α-1,4 glycosidic bonds.

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Amylopectin

Branched starch with α-1,4 and α-1,6 glycosidic bonds.

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Glycogen

Animal storage form of glucose, similar to amylopectin but more branched.

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Cellulose

Structural component in plants with β-1,4 glycosidic bonds.

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Pyruvate Dehydrogenase Complex (PDC)

Conversion of pyruvate to acetyl-CoA for Krebs cycle under aerobic conditions.

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Lactate Dehydrogenase

Converts pyruvate to lactate under anaerobic conditions, regenerating NAD+.

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Citrate Synthase

Enzyme that catalyzes the first step of Krebs cycle by combining Acetyl-CoA and Oxaloacetate to form Citrate.

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Net ATP Gain (Glycolysis to Pyruvate)

Energy yield of glycolysis to pyruvate.

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Glycogen Phosphorylase

Enzyme that removes glucose from the non-reducing ends of glycogen.

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Debranching Enzyme

Enzyme that shifts 3 glucose residues and hydrolyzes branch point glucose in glycogenolysis.

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Phosphoglucomutase

Converts Glucose-1-Phosphate to Glucose-6-Phosphate.

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Glycogen Synthase

Enzyme that forms α(1→4) glycosidic bonds in glycogen synthesis.

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Branching Enzyme

Introduces α(1→6) branches in glycogen synthesis.

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Oxidative Stage of Pentose Phosphate Pathway

The main reactions of the first oxidative stage in the pentose phosphate pathway.

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Glucose-6-Phosphate Dehydrogenase (G6PD)

Enzyme that converts Glucose-6-Phosphate to Ribulose-5-Phosphate.

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Lactate

Three carbon molecule from anaerobic glycolysis.

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Absorptive State

The state when the body gets energy by oxidizing nutrients absorbed from the intestine.

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Postabsorptive State

State when the body mobilizes energy from body stores.

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Liver Glucose Production

The liver produces glucose via glycogenolysis and gluconeogenesis.

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Insulin

Hormone that lowers glucose and fatty acids in plasma.

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Glucagon

Hormone that stimulates glycogenolysis and gluconeogenesis.

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Metabolic Rate

The total energy turnover in the body per unit time.

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Respiratory Quotient (RQ)

The ratio of CO2 produced to O2 consumed, indicating which energy substrate is being used.

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Heat increment of digestion

Increase in heat production after eating.

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Aerobic Metabolic Scope

The ratio of maximum metabolic rate to maintenance metabolic rate.

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Study Notes

Digestion of Carbohydrates

  • Monosaccharides are the simplest carbohydrates and cannot be further hydrolyzed
  • Examples of monosaccharides include Glucose, Fructose, and Galactose
  • Disaccharides are composed of two monosaccharide units
  • Examples of disaccharides include Maltose (Glucose + Glucose), Lactose (Glucose + Galactose), and Sucrose (Glucose + Fructose)
  • Oligosaccharides contain a small number (2-10) of monosaccharide units
  • Polysaccharides are large polymers of monosaccharides
  • Examples of polysaccharides include Starch, Glycogen, and Cellulose

Lipid Digestion

  • Focus on enzymes, location, products, emulsification, bile acid function, and absorption

Monosaccharides

  • Monosaccharides exist in both linear (Fischer projection) and cyclic (Haworth projection) forms
  • Cyclic structures form due to hemiacetal or hemiketal formation
  • Glucose forms a six-membered pyranose ring.
  • Fructose forms a five-membered furanose ring

Protein Digestion

  • Focus on enzymes, location, and products

Physical Properties

  • Colorless, crystalline solids that are soluble in water but insoluble in nonpolar solvents

Chemical Properties

  • Can be oxidized to form carboxylic acids
  • Can be reduced to form sugar alcohols (e.g., glucose → sorbitol)
  • Can form glycosidic bonds to create disaccharides and polysaccharides

Enzymes, Location, and Products

  • Stomach: Pepsin (activated by HCl) hydrolyzes proteins into polypeptides
  • Small Intestine:
    • Pancreatic Proteases:
      • Trypsin & Chymotrypsin: Cleave peptide bonds into smaller peptides
      • Carboxypeptidase: Removes terminal amino acids
      • Aminopeptidase & Dipeptidase: Cleave peptides into free amino acids
    • Absorption: Free amino acids are absorbed via Na+-dependent active transport

Protein Digestion in Ruminants vs. Non-Ruminants

  • Ruminants:
    • Rumen microbes digest dietary protein, producing microbial protein
    • Microbial proteases degrade proteins into peptides & ammonia
    • Microbes synthesize new proteins from ammonia and volatile fatty acids
    • Rumen Undegradable Protein (RUP) passes to the small intestine for absorption
  • Non-Ruminants: Rely on gastric and pancreatic enzymes for protein digestion

Material Transfer and Membranes

  • Focus on chemical composition, function, structural elements (proteins, carbohydrates, and lipids) of membranes, types of transport, and examples

Chemical Composition of Membranes

  • Composed of lipids, proteins, and carbohydrates
  • Lipids consist of phospholipids, sphingolipids, and cholesterol
  • Proteins include integral and peripheral proteins
  • Carbohydrates are present as glycolipids and glycoproteins, important for cell recognition

Structural Elements of Membranes

  • Phospholipid Bilayer: Hydrophilic heads face outward, hydrophobic tails face inward
  • Proteins:
    • Integral Proteins: Embedded in the membrane, help in transport
    • Peripheral Proteins: Attached to membrane surfaces, involved in signaling
  • Carbohydrates: Attached to proteins (glycoproteins) or lipids (glycolipids), crucial for cell recognition

Types of Membrane Transport

  • Passive Transport (No energy required)
    • Diffusion: Movement from high to low concentration
    • Facilitated Diffusion: Uses carrier or channel proteins
    • Osmosis: Water movement through the membrane (via aquaporins)
  • Active Transport (Requires energy – ATP)
    • Primary Active Transport: Direct use of ATP (e.g., Sodium-Potassium (Na+/K+) Pump: 3 Na+ out, 2 K+ in)
    • Secondary Active Transport: Uses energy from another molecule's concentration gradient (e.g., glucose transport)
  • Endocytosis & Exocytosis (Bulk Transport)
    • Endocytosis: Engulfing substances into the cell
    • Exocytosis: Releasing substances out of the cell

Carbohydrates

  • Focus on classification, linear and cyclic structures, properties, reducing/non-reducing disaccharides/polysaccharides, bonds, qualitative tests of carbohydrates
  • Starch (plant storage form of glucose)
  • Amylose: Unbranched, α-1,4 glycosidic bonds
  • Amylopectin: Branched, α-1,4 and α-1,6 glycosidic bonds
  • Glycogen (animal storage form of glucose): Similar to amylopectin but more highly branched (every 8–12 glucose units)
  • Cellulose (structural component in plants): β-1,4 glycosidic bonds; indigestible by humans

Glycolysis

  • Focus on the first and second stages of glycolysis: Reactions, enzymes, energy producing or using reactions

Fehling's/Benedict's Test

  • For reducing sugars; positive result is a brick-red precipitate (Cu2O)

Iodine Test

  • For starch detection; starch reacts with iodine to give a blue-black color; glycogen may give a reddish-brown color

Stages and Reactions

  • Stage 1: Energy Investment Phase (Reactions 1-5)
    • Glucose → Glucose-6-Phosphate (G6P)
      • Enzyme: Hexokinase/Glucokinase (in liver)
      • Consumes 1 ATP
    • G6P → Fructose-6-Phosphate (F6P)
      • Enzyme: Phosphoglucose Isomerase
    • F6P → Fructose-1,6-Bisphosphate (F1,6BP)
      • Enzyme: Phosphofructokinase-1 (PFK-1)
      • Consumes 1 ATP
    • F1,6BP → Glyceraldehyde-3-Phosphate (G3P) + Dihydroxyacetone Phosphate (DHAP)
      • Enzyme: Aldolase
    • DHAP → G3P
      • Enzyme: Triose Phosphate Isomerase
  • Net: -2 ATP used
  • Stage 2: Energy Payoff Phase (Reactions 6-10)
    • G3P → 1,3-Bisphosphoglycerate (1,3-BPG)
      • Enzyme: Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH)
      • Produces NADH
    • 1,3-BPG → 3-Phosphoglycerate (3PG)
      • Enzyme: Phosphoglycerate Kinase
      • Generates 2 ATP (substrate-level phosphorylation)
    • 3PG → 2-Phosphoglycerate (2PG)
      • Enzyme: Phosphoglycerate Mutase
    • 2PG → Phosphoenolpyruvate (PEP)
      • Enzyme: Enolase
    • PEP → Pyruvate
      • Enzyme: Pyruvate Kinase
      • Generates 2 ATP (substrate-level phosphorylation)
  • Net: +4 ATP, +2 NADH, +2 Pyruvate
  • Overall ATP Yield: +2 ATP per glucose

Pyruvate

  • Focus on fates in aerobic and anaerobic conditions: Conditions, main reason of lactate production, reactions, enzymes, products

Aerobic Conditions

  • Pyruvate is converted into Acetyl-CoA by the Pyruvate Dehydrogenase Complex (PDC)
  • Acetyl-CoA enters the Krebs cycle (Citric Acid Cycle) for further oxidation
  • Products: CO2, NADH, and Acetyl-CoA

Anaerobic Conditions

  • Pyruvate is converted into Lactate by Lactate Dehydrogenase
  • This regenerates NAD+, allowing glycolysis to continue
  • Main reason for lactate production: To regenerate NAD+ for glycolysis in the absence of oxygen

Oxidative Decarboxylation of Pyruvate

  • Focus on enzymes, coenzymes, mechanism, products, regenerated/non-regenerated coenzymes

Enzymes and Coenzymes

  • Enzyme Complex: Pyruvate Dehydrogenase Complex (PDC)
  • Coenzymes Involved:
    • Thiamine Pyrophosphate (TPP) – (Bound to E1)
    • Lipoamide – (Bound to E2)
    • Coenzyme A (CoA) – (Substrate for E2)
    • FAD (Flavin Adenine Dinucleotide) – (Bound to E3)
    • NAD (Nicotinamide Adenine Dinucleotide) – (Substrate for E3)

Mechanism of Reaction

  • E1: Pyruvate Decarboxylation
    • Pyruvate reacts with TPP, leading to the formation of Hydroxyethyl-TPP
    • CO2 is released
  • E2: Acetyl Transfer to CoA
    • The hydroxyethyl group is oxidized and transferred to lipoamide
    • The acetyl group is then transferred to Coenzyme A (CoA) forming Acetyl-CoA
  • E3: Regeneration of Lipoamide
    • FAD oxidizes lipoamide, regenerating its disulfide form
    • NAD+ oxidizes FADH2, producing NADH + H+

Products

  • Acetyl-CoA (enters the Krebs Cycle)
  • NADH (goes to the electron transport chain)
  • CO2 (exhaled as a waste product)

Regenerated and Non-Regenerated Coenzymes

  • Regenerated: Lipoamide, FAD
  • Non-Regenerated: NADH, Acetyl-CoA

Krebs Cycle

  • Focus on precursors and products, reactions and enzymes, reactions where energy is produced, and reactions where oxidative decarboxylation occurs

Reactions and Enzymes

  • Acetyl-CoA + Oxaloacetate → Citrate
    • Enzyme: Citrate Synthase
  • Citrate → Isocitrate
    • Enzyme: Aconitase
  • Isocitrate → α-Ketoglutarate (Oxidative Decarboxylation, Produces NADH)
    • Enzyme: Isocitrate Dehydrogenase
  • α-Ketoglutarate → Succinyl-CoA (Oxidative Decarboxylation, Produces NADH)
    • Enzyme: α-Ketoglutarate Dehydrogenase
  • Succinyl-CoA → Succinate (Substrate-Level Phosphorylation, Produces GTP/ATP)
    • Enzyme: Succinyl-CoA Synthetase
  • Succinate → Fumarate (Produces FADH2)
    • Enzyme: Succinate Dehydrogenase
  • Fumarate → Malate
    • Enzyme: Fumarase
  • Malate → Oxaloacetate (Produces NADH)
    • Enzyme: Malate Dehydrogenase

Energy-Producing Reactions

  • NADH-producing reactions:
    • Isocitrate → α-Ketoglutarate
    • α-Ketoglutarate → Succinyl-CoA
    • Malate → Oxaloacetate
  • FADH2-producing reaction:
    • Succinate → Fumarate
  • ATP/GTP-producing reaction:
    • Succinyl-CoA → Succinate

Energy Yield of Glycolysis

  • Focus on energy yield to pyruvate; to lactate; and to CO2/H2O

To Pyruvate

  • Net ATP Gain: 2 ATP
  • NADH Produced: 2 NADH

To Lactate

  • 2 ATP (same as pyruvate stage, NADH is used to convert pyruvate to lactate)

To CO2 and H2O (Complete Oxidation)

  • Glycolysis: 2 ATP, 2 NADH (5 ATP)
  • Krebs Cycle (Per Glucose): 2 GTP, 6 NADH (15 ATP), 2 FADH2 (3 ATP)
  • Total ATP Yield: ~30-32 ATP per glucose

Glycolysis to Pyruvate

  • 2 ATP (net)
  • 2 NADH (5 ATP if fully oxidized in mitochondria)

Glycolysis to Lactate (Anaerobic)

  • 2 ATP (since NADH is used in lactate formation, no additional ATP)

Complete Oxidation to CO2 & H2O

  • Glycolysis: 2 ATP + 2 NADH (5 ATP)
  • Pyruvate → Acetyl-CoA: 2 NADH (5 ATP)
  • Krebs Cycle (2 rounds): 6 NADH (15 ATP), 2 FADH2 (3 ATP), 2 GTP (2 ATP)
  • Total: ~30-32 ATP per glucose molecule

Final Energy Yield

  • Glycolysis → Pyruvate: 8 ATP
  • Pyruvate → Acetyl-CoA: 6 ATP
  • Acetyl-CoA → CO2 + H2O (Krebs Cycle): 24 ATP
  • Total ATP (Complete Oxidation of Glucose): 38 ATP

Glycogenolysis

  • Focus on stages, enzymes, debranching, and products

Stages & Enzymes

  • Glycogen Phosphorylase:
    • Removes glucose from the non-reducing ends
    • Converts glycogen → Glucose-1-Phosphate
    • Stops 4 residues before a branch point
  • Debranching Enzyme:
    • α(1,4) Transglycosylase shifts 3 glucose residues
    • α(1,6) Glucosidase hydrolyzes branch point glucose → Free Glucose
  • Phosphoglucomutase:
    • Converts Glucose-1-Phosphate → Glucose-6-Phosphate

Products

  • Glucose-6-Phosphate (for glycolysis or blood glucose regulation)
  • Free Glucose (from branch points)

Glycogen Synthesis

  • Focus on stages, enzymes, and branching
  • Stages:
    • Glucose → Glucose-1-P (Enzyme: Phosphoglucomutase)
    • Glucose-1-P + UTP → UDP-Glucose (Enzyme: UDP-Glucose Pyrophosphorylase)
    • Glycogen Synthase forms α(1→4) glycosidic bonds
    • Branching Enzyme introduces α(1→6) branches

Pentose Phosphate Pathway

  • Focus on stages, main reactions of the first oxidative stage, enzymes, and functions (NADPH, glutathione, glucose-6-phosphate dehydrogenase)

Stages & Reactions

  • Oxidative Stage (Irreversible)
    • Glucose-6-Phosphate → Ribulose-5-Phosphate
      • Enzyme: Glucose-6-Phosphate Dehydrogenase (G6PD)
      • Products: NADPH & CO2
  • Non-Oxidative Stage (Reversible)
    • Converts 3-7 carbon sugars for biosynthetic use
    • Provides Ribose-5-Phosphate for nucleotide synthesis

Functions

  • NADPH production:
    • Used for fatty acid synthesis (liver, adipose tissue)
    • Maintains glutathione in its reduced form (antioxidant in RBCs)
  • Glucose-6-Phosphate Dehydrogenase Deficiency:
    • Leads to hemolysis in RBCs due to oxidative stress

Gluconeogenesis

  • Focus on similarities/differences between glycolysis/gluconeogenesis & non-reversible reactions/enzymes

Differences from Glycolysis

  • Not a simple reversal of glycolysis
  • Bypasses 3 irreversible steps:
  1. Pyruvate → Phosphoenolpyruvate (PEP):
  • Pyruvate Carboxylase converts Pyruvate → Oxaloacetate
  • PEP Carboxykinase (PEPCK) converts Oxaloacetate → PEP
  1. Fructose-1,6-Bisphosphate → Fructose-6-Phosphate:
  • Enzyme: Fructose-1,6-Bisphosphatase
  1. Glucose-6-Phosphate → Glucose:
  • Enzyme: Glucose-6-Phosphatase (in ER of liver/kidney)

Precursors for Glucose Synthesis

  • Lactate (from anaerobic glycolysis)
  • Amino Acids (mainly Alanine)
  • Glycerol (from triglyceride breakdown)

Metabolism

  • Focus on energy/substance transformations, anabolic/catabolic processes, ATP structure, ATP's role in energy metabolism

ATP Structure

  • Adenine + Ribose + Three Phosphate groups

Role

  • Anabolic Reactions: Provides energy for biosynthesis
  • Catabolic Reactions: ATP is regenerated via glycolysis, Krebs cycle, and oxidative phosphorylation

Substrate-Level Phosphorylation

  • Focus on macroergic compounds and examples
  • Definition & Mechanism: Substrate-level phosphorylation is the direct formation of ATP by transferring a phosphoryl group from a high-energy intermediate to ADP
  • This process does not require oxygen and occurs in:
    • Glycolysis
    • Krebs Cycle (TCA Cycle)

Examples

  • Glycolysis:
    • 1,3-Bisphosphoglycerate + ADP → 3-Phosphoglycerate + ATP
      • Enzyme: Phosphoglycerate Kinase
    • Phosphoenolpyruvate (PEP) + ADP → Pyruvate + ATP
      • Enzyme: Pyruvate Kinase
  • Krebs Cycle:
    • Succinyl-CoA + GDP → Succinate + GTP
    • Enzyme: Succinyl-CoA Synthetase

Oxidative Phosphorylation

  • Focus on respiratory chain enzymes, their localization in the cell, respiratory chain dehydrogenases/cytochrome coenzymes, their structure, equations of redox reactions in the respiratory chain, and proton transport across the membrane
  • Definition: Oxidative phosphorylation is the formation of ATP using energy derived from the transfer of electrons in the Electron Transport Chain (ETC)
  • Requires oxygen as the final electron acceptor

Enzymes & Complexes in the Respiratory Chain

  • Complex I (NADH-CoQ Reductase): Transfers electrons from NADH → Coenzyme Q (Ubiquinone); pumps 4 H+ into the intermembrane space
  • Complex II (Succinate-CoQ Reductase): Transfers electrons from FADH2 → Coenzyme Q; does not pump protons
  • Complex III (CoQ-Cytochrome c Reductase): Transfers electrons from CoQ → Cytochrome c; pumps 4 H+
  • Complex IV (Cytochrome c Oxidase): Transfers electrons from Cytochrome c → O2; final step: O2 is reduced to H2O; pumps 2 H+

Proton Transport & ATP Synthesis

  • Electron movement generates a proton gradient across the inner mitochondrial membrane
  • This creates the proton motive force (PMF)
  • ATP Synthase (Complex V) uses this gradient to produce ATP

ATP Synthase

  • Focus on the principle of action and energy effect of oxidation of reduced dehydrogenases

Mechanism of ATP Synthase

  • Location: Inner mitochondrial membrane
  • Structure:
    • Fo Subunit: Proton channel that allows H+ back into the matrix
    • F1 Subunit: Catalyzes ATP synthesis from ADP + Pi
  • Mechanism (Chemiosmotic Theory)
    • Protons flow through Fo due to the proton gradient
    • F1 subunit rotates, inducing conformational changes
    • ATP is synthesized from ADP and Pi

Energy Yield of Oxidative Phosphorylation

  • NADH oxidation → 3 ATP
  • FADH2 oxidation → 2 ATP
  • Total ATP yield per glucose molecule (including glycolysis, Krebs cycle, oxidative phosphorylation) = 38 ATP

Utilization of Organic Nutrients

  • Focus on metabolism of organic nutrients, absorptive and postabsorptive states, and carbohydrate/protein/lipid metabolism

Metabolism

  • Refers to all chemical reactions in the body
  • Consists of:
    • Catabolism: Breaking down complex molecules to release energy
    • Anabolism: Using energy to synthesize large molecules

Energy Source

  • During digestion, energy is transferred to the body as glucose, fatty acids, and amino acids
  • Some molecules are used for synthesis, while others are oxidized, producing CO2, H2O, and heat

Absorptive State (Anabolic)

  • Body gets energy by oxidizing nutrients absorbed from the intestine
  • Carbohydrates, fats, and proteins are used for growth and energy storage

Postabsorptive State (Catabolic)

  • Energy is mobilized from body stores
  • Liver produces glucose via Glycogenolysis (breakdown of glycogen) & Gluconeogenesis (conversion of lactate, pyruvate, amino acids, and glycerol into glucose)

Carbohydrate Metabolism

  • Non-Ruminants: Starch/glycogen broken into monosaccharides (glucose, galactose, fructose); glucose is main monosaccharide absorbed
  • Herbivores: Cellulose is the main carbohydrate
  • Ruminants: Cellulose is converted to volatile fatty acids (VFAs) by microbes
  • Simple-Stomached Herbivores: Cellulose metabolism occurs in the large intestine

Liver's Role

  • Stores glucose as glycogen or converts it to lipids
  • Maintains blood glucose levels through Glycogenolysis and Gluconeogenesis
  • Glucose sparing (using lipids as energy)

Protein Metabolism

  • Liver Functions:
    • Converts amino acids to glucose or fatty acids
    • Produces albumin, enzymes, and clotting factors
    • Deamination: Converts amino acids to keto acids, used for energy or stored as fat
    • Transamination: Converts amino acids into non-essential amino acids
    • Urea Cycle: Converts toxic ammonia (NH3) into urea for excretion
  • Ruminants: Microbial proteins are synthesized in the forestomach; dietary amino acid composition is less important

Lipids Metabolism

  • Triglycerides are the major storage form of energy
  • Lipids are transported in the blood
  • Chylomicrons transport dietary lipids
  • VLDL (Very Low-Density Lipoproteins) transport liver-produced lipids

Lipid Metabolism

  • Lipolysis releases fatty acids for energy
  • Glucose Sparing: During fasting, tissues switch to fat metabolism

Regulation of Organic Nutrient Metabolism

  • Hormonal Control:
    • Insulin: Lowers glucose and fatty acids in plasma
    • Glucagon: Stimulates glycogenolysis and gluconeogenesis
    • Cortisol: Stimulates gluconeogenesis
    • Epinephrine: Stimulates glycogenolysis
    • Growth Hormone: Mobilizes fatty acids
  • Nervous System Control:
    • Sympathetic Nervous System: Increases glucose release
    • Parasympathetic Nervous System: Stimulates insulin secretion

Regulation of Body Temperature

  • Normal body temperature in mammals: 36.5–39.5°C (varies by species) & Birds: 38-42°C
  • Measurement: Usually taken rectally with an electronic or liquid thermometer
  • Hyperthermia is excess heat production or reduced heat loss
    • Occurs during exercise, infections (fever), pregnancy, and lactation
  • Hypothermia is when heat loss exceeds heat production
    • Common in newborns, old animals, and small breeds
    • Risk factors: Wet fur, prolonged exposure to cold, and inadequate fat/hair coat

Clinical Signs of Hypothermia

  • Shivering, slow breathing, lethargy, and low blood pressure
  • Severe cases: Muscle stiffness, dilated pupils, and coma

Heat Balance

  • Balance between heat production and heat loss to maintain body temperature, heat input must equal heat output

Heat Production

  • Basal metabolism: The body's normal energy use
  • Shivering: Involuntary muscle contractions to generate heat
  • Non-Shivering Thermogenesis: Brown Adipose Tissue (BAT) is present in newborns and hibernating animals
  • Sympathetic Nervous System increases fat oxidation
  • Thyroid Hormones increase metabolism and heat production

Heat Loss Mechanisms

  • Radiation: Heat transfer by electromagnetic waves
  • Conduction: Heat transfer via direct contact with objects
  • Convection: Heat loss through moving air/water
  • Evaporation: Sweating, panting, and wetting body surface

Thermoneutral Zone

  • The most energy-efficient temperature range for an animal
  • Outside the TNZ:
    • Too warm → Body must spend energy on cooling
    • Too cold → Body must spend energy on warming

Extreme Heat/Cold Conditions

  • Hibernation: Some mammals lower body temperature to 4-8°C in winter
  • Estivation: Heat dormancy in hot climates
  • Body Temperature Regulation: Controlled by Reflexes:
    • Sensory Input: Skin, internal organs, and hypothalamus detect temperature changes
    • Integrating Center: Hypothalamus regulates body temperature
    • Motor Output:
      • Heat Stress: Sweating, panting, and increased blood flow to skin
      • Cold Stress: Shivering, reduced blood flow to skin, and increased hormone secretion

Bioenergetics and Growth

  • Focus on absorption of energy substrates and metabolic rate
  • Energy intake = Energy expenditure to maintain body functions

Energy Substrates

  • Carbohydrates: Provide 4.1 kcal/gram
  • Proteins: Provide 4.1 kcal/gram
  • Lipids (Fats): Provide 9.3 kcal/gram

Metabolic Rate

  • The total energy turnover in the body per unit time
  • Factors affecting metabolic rate:
    • Body size (smaller animals have higher metabolic rates per unit weight)
    • Physical activity (exercise increases metabolism)
    • Environmental temperature (increases when cold or hot)
    • Reproductive status (pregnancy, lactation)
    • Hormones: Thyroid hormones/sympathetic nervous system increase metabolic rate
    • Starvation lowers metabolic rate.

Metabolic Rate Types

  • Basal Metabolic Rate (BMR): Minimum energy required for basic life functions
  • Fasting Metabolic Rate: Energy expenditure when an animal can move but is fasting
  • Maintenance Metabolic Rate: Energy required to maintain body mass without production
  • Field Metabolic Rate: Average daily metabolic rate under natural conditions

Energy Requirements

  • Calculation of energy requirements of animals
  • Production animals (e.g., dairy cows, laying hens, horses) require extra energy for work, growth, and milk/wool/egg production
  • Formula: Total Energy Requirement = Maintenance Energy + Production Energy
  • Measurement of metabolic rate.

Respiratory Quotient

  • Definition: The ratio of CO2 produced / O2 consumed
  • Indicates which energy substrate is being used:
    • Carbohydrates → RQ = 1.0
    • Proteins → RQ = 0.8
    • Lipids → RQ = 0.7
    • RQ > 1: Suggests anaerobic respiration is occurring

Heat Increment Digestion

  • Definition: Increase in heat production after eating
  • High in ruminants (50% of metabolizable energy due to fermentation)
  • Lower in simple-stomached animals (10-30%)

Aerobic Metabolic Scope

  • Definition: The ratio of maximum metabolic rate / maintenance metabolic rate
  • During intense activity, animals can increase metabolic rate 25-35 times

Feed Energy Utilization

  • Carnivores: Digest meat and fat efficiently (>80% metabolizable energy)
  • Herbivores: Lose ~50% of feed energy in feces, urine, and methane
  • Omnivores (e.g., pigs): Have energy utilization between herbivores and carnivores

Energy Storage

  • Excess energy is stored as triglycerides

Energy Storage Examples

  • Deer: Use fat stores for winter survival
  • Migratory birds: Store fat before migration
  • Lactating mammals: Use fat reserves for milk production
  • Growth requires ATP (energy source) and nutrients for cell building (proteins, lipids, minerals)
  • Fetal Growth:
    • Mammals: Nutrients come from the placenta
    • Birds: Nutrients come from the egg yolk
  • Hormonal Control:
    • Fetal Stage: Insulin and T3 regulate growth
    • Postnatal Growth: Growth Hormone (GH) and Insulin-Like Growth Factor (IGF)

Aging Effects

  • Reduced appetite, metabolic rate, muscle mass, and mental ability
  • Cell number decreases over time
  • Production animals are slaughtered before aging effects occur
  • Companion animals/herbivores live longer and experience aging diseases.
  • Aging accelerates when teeth wear down, affecting digestion

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