Raffi Hovasapian
Amino Acid Catabolism
Slide Duration:Table of Contents
39m 57s
- Intro0:00
- Aqueous Solutions and Concentration0:46
- Definition of Solution1:28
- Example: Sugar Dissolved in Water2:19
- Example: Salt Dissolved in Water3:04
- A Solute Does Not Have to Be a Solid3:37
- A Solvent Does Not Have to Be a Liquid5:02
- Covalent Compounds6:55
- Ionic Compounds7:39
- Example: Table Sugar9:12
- Example: MgCl₂10:40
- Expressing Concentration: Molarity13:42
- Example 114:47
- Example 1: Question14:50
- Example 1: Solution15:40
- Another Way to Express Concentration22:01
- Example 224:00
- Example 2: Question24:01
- Example 2: Solution24:49
- Some Other Ways of Expressing Concentration27:52
- Example 329:30
- Example 3: Question29:31
- Example 3: Solution31:02
38m 53s
- Intro0:00
- Dilution0:45
- Definition of Dilution0:46
- Example 1: Question2:08
- Example 1: Basic Dilution Equation4:20
- Example 1: Solution5:31
- Example 2: Alternative Approach12:05
- Osmotic Pressure14:34
- Colligative Properties15:02
- Recall: Covalent Compounds and Soluble Ionic Compounds17:24
- Properties of Pure Water19:42
- Addition of a Solute21:56
- Osmotic Pressure: Conceptual Example24:00
- Equation for Osmotic Pressure29:30
- Example of 'i'31:38
- Example 332:50
29m 1s
- Intro0:00
- More on Osmosis1:25
- Osmotic Pressure1:26
- Example 1: Molar Mass of Protein5:25
- Definition, Equation, and Unit of Osmolarity13:13
- Example 2: Osmolarity15:19
- Isotonic, Hypertonic, and Hypotonic20:20
- Example 322:20
- More on Isotonic, Hypertonic, and Hypotonic26:14
- Osmosis vs. Osmotic Pressure27:56
39m 11s
- Intro0:00
- Acids and Bases1:16
- Let's Begin With H₂O1:17
- P-Scale4:22
- Example 16:39
- pH9:43
- Strong Acids11:10
- Strong Bases13:52
- Weak Acids & Bases Overview14:32
- Weak Acids15:49
- Example 2: Phosphoric Acid19:30
- Weak Bases24:50
- Weak Base Produces Hydroxide Indirectly25:41
- Example 3: Pyridine29:07
- Acid Form and Base Form32:02
- Acid Reaction35:50
- Base Reaction36:27
- Ka, Kb, and Kw37:14
41m 33s
- Intro0:00
- Titrations0:27
- Weak Acid0:28
- Rearranging the Ka Equation1:45
- Henderson-Hasselbalch Equation3:52
- Fundamental Reaction of Acids and Bases5:36
- The Idea Behind a Titration6:27
- Let's Look at an Acetic Acid Solution8:44
- Titration Curve17:00
- Acetate23:57
- Buffers26:57
- Introduction to Buffers26:58
- What is a Buffer?29:40
- Titration Curve & Buffer Region31:44
- How a Buffer Works: Adding OH⁻34:44
- How a Buffer Works: Adding H⁺35:58
- Phosphate Buffer System38:02
44m 19s
- Intro0:00
- Example 11:21
- Example 1: Properties of Glycine1:22
- Example 1: Part A3:40
- Example 1: Part B4:40
- Example 29:02
- Example 2: Question9:03
- Example 2: Total Phosphate Concentration12:23
- Example 2: Final Solution17:10
- Example 319:34
- Example 3: Question19:35
- Example 3: pH Before22:18
- Example 3: pH After24:24
- Example 3: New pH27:54
- Example 430:00
- Example 4: Question30:01
- Example 4: Equilibria32:52
- Example 4: 1st Reaction38:04
- Example 4: 2nd Reaction39:53
- Example 4: Final Solution41:33
18m 45s
- Intro0:00
- Hydrolysis and Condensation Reactions0:50
- Hydrolysis0:51
- Condensation2:42
- Example 1: Hydrolysis of Ethyl Acetate4:52
- Example 2: Condensation of Acetic Acid with Ethanol8:42
- Example 311:18
- Example 4: Formation & Hydrolysis of a Peptide Bond Between the Amino Acids Alanine & Serine14:56
38m 19s
- Intro0:00
- Amino Acids0:17
- Proteins & Amino Acids0:18
- Difference Between Amino Acids4:20
- α-Carbon7:08
- Configuration in Biochemistry10:43
- L-Glyceraldehyde & Fischer Projection12:32
- D-Glyceraldehyde & Fischer Projection15:31
- Amino Acids in Biological Proteins are the L Enantiomer16:50
- L-Amino Acid18:04
- L-Amino Acids Correspond to S-Enantiomers in the RS System20:10
- Classification of Amino Acids22:53
- Amino Acids With Non-Polar R Groups26:45
- Glycine27:00
- Alanine27:48
- Valine28:15
- Leucine28:58
- Proline31:08
- Isoleucine32:42
- Methionine33:43
- Amino Acids With Aromatic R Groups34:33
- Phenylalanine35:26
- Tyrosine36:02
- Tryptophan36:32
27m 14s
- Intro0:00
- Amino Acids With Positively Charged R Groups0:16
- Lysine0:52
- Arginine1:55
- Histidine3:15
- Amino Acids With Negatively Charged R Groups6:28
- Aspartate6:58
- Glutamate8:11
- Amino Acids With Uncharged, but Polar R Groups8:50
- Serine8:51
- Threonine10:21
- Cysteine11:06
- Asparagine11:35
- Glutamine12:44
- More on Amino Acids14:18
- Cysteine Dimerizes to Form Cystine14:53
- Tryptophan, Tyrosine, and Phenylalanine19:07
- Other Amino Acids20:53
- Other Amino Acids: Hydroxy Lysine22:34
- Other Amino Acids: r-Carboxy Glutamate25:37
48m 28s
- Intro0:00
- Acid/Base Behavior of Amino Acids0:27
- Acid/Base Behavior of Amino Acids0:28
- Let's Look at Alanine1:57
- Titration of Acidic Solution of Alanine with a Strong Base2:51
- Amphoteric Amino Acids13:24
- Zwitterion & Isoelectric Point16:42
- Some Amino Acids Have 3 Ionizable Groups20:35
- Example: Aspartate24:44
- Example: Tyrosine28:50
- Rule of Thumb33:04
- Basis for the Rule35:59
- Example: Describe the Degree of Protonation for Each Ionizable Group38:46
- Histidine is Special44:58
45m 18s
- Intro0:00
- Peptides and Proteins0:15
- Introduction to Peptides and Proteins0:16
- Formation of a Peptide Bond: The Bond Between 2 Amino Acids1:44
- Equilibrium7:53
- Example 1: Build the Following Tripeptide Ala-Tyr-Ile9:48
- Example 1: Shape Structure15:43
- Example 1: Line Structure17:11
- Peptides Bonds20:08
- Terms We'll Be Using Interchangeably23:14
- Biological Activity & Size of a Peptide24:58
- Multi-Subunit Proteins30:08
- Proteins and Prosthetic Groups32:13
- Carbonic Anhydrase37:35
- Primary, Secondary, Tertiary, and Quaternary Structure of Proteins40:26
42m 47s
- Intro0:00
- Amino Acid Sequencing of a Peptide Chain0:30
- Amino Acid Sequence and Its Structure0:31
- Edman Degradation: Overview2:57
- Edman Degradation: Reaction - Part 14:58
- Edman Degradation: Reaction - Part 210:28
- Edman Degradation: Reaction - Part 313:51
- Mechanism Step 1: PTC (Phenylthiocarbamyl) Formation19:01
- Mechanism Step 2: Ring Formation & Peptide Bond Cleavage23:03
- Example: Write Out the Edman Degradation for the Tripeptide Ala-Tyr-Ser30:29
- Step 130:30
- Step 234:21
- Step 336:56
- Step 438:28
- Step 539:24
- Step 640:44
1h 2m 33s
- Intro0:00
- Sequencing Larger Peptides and Proteins0:28
- Identifying the N-Terminal Amino Acids With the Reagent Fluorodinitrobenzene (FDNB)0:29
- Sequencing Longer Peptides & Proteins Overview5:54
- Breaking Peptide Bond: Proteases and Chemicals8:16
- Some Enzymes/Chemicals Used for Fragmentation: Trypsin11:14
- Some Enzymes/Chemicals Used for Fragmentation: Chymotrypsin13:02
- Some Enzymes/Chemicals Used for Fragmentation: Cyanogen Bromide13:28
- Some Enzymes/Chemicals Used for Fragmentation: Pepsin13:44
- Cleavage Location14:04
- Example: Chymotrypsin16:44
- Example: Pepsin18:17
- More on Sequencing Larger Peptides and Proteins19:29
- Breaking Disulfide Bonds: Performic Acid26:08
- Breaking Disulfide Bonds: Dithiothreitol Followed by Iodoacetate31:04
- Example: Sequencing Larger Peptides and Proteins37:03
- Part 1 - Breaking Disulfide Bonds, Hydrolysis and Separation37:04
- Part 2 - N-Terminal Identification44:16
- Part 3 - Sequencing Using Pepsin46:43
- Part 4 - Sequencing Using Cyanogen Bromide52:02
- Part 5 - Final Sequence56:48
49m 12s
- Intro0:00
- Peptide Synthesis (Merrifield Process)0:31
- Introduction to Synthesizing Peptides0:32
- Merrifield Peptide Synthesis: General Scheme3:03
- So What Do We Do?6:07
- Synthesis of Protein in the Body Vs. The Merrifield Process7:40
- Example: Synthesis of Ala-Gly-Ser9:21
- Synthesis of Ala-Gly-Ser: Reactions Overview11:41
- Synthesis of Ala-Gly-Ser: Reaction 119:34
- Synthesis of Ala-Gly-Ser: Reaction 224:34
- Synthesis of Ala-Gly-Ser: Reaction 327:34
- Synthesis of Ala-Gly-Ser: Reaction 4 & 4a28:48
- Synthesis of Ala-Gly-Ser: Reaction 533:38
- Synthesis of Ala-Gly-Ser: Reaction 636:45
- Synthesis of Ala-Gly-Ser: Reaction 7 & 7a37:44
- Synthesis of Ala-Gly-Ser: Reaction 839:47
- Synthesis of Ala-Gly-Ser: Reaction 9 & 1043:23
- Chromatography: Eluent, Stationary Phase, and Eluate45:55
54m 31s
- Intro0:00
- Example 10:22
- Data0:23
- Part A: What is the pI of Serine & Draw the Correct Structure2:11
- Part B: How Many mL of NaOH Solution Have Been Added at This Point (pI)?5:27
- Part C: At What pH is the Average Charge on Serine10:50
- Part D: Draw the Titration Curve for This Situation14:50
- Part E: The 10 mL of NaOH Added to the Solution at the pI is How Many Equivalents?17:35
- Part F: Serine Buffer Solution20:22
- Example 223:04
- Data23:05
- Part A: Calculate the Minimum Molar Mass of the Protein25:12
- Part B: How Many Tyr Residues in this Protein?28:34
- Example 330:08
- Question30:09
- Solution34:30
- Example 448:46
- Question48:47
- Solution49:50
50m 52s
- Intro0:00
- Alpha Helix and Beta Conformation0:28
- Protein Structure Overview0:29
- Weak interactions Among the Amino Acid in the Peptide Chain2:11
- Two Principals of Folding Patterns4:56
- Peptide Bond7:00
- Peptide Bond: Resonance9:46
- Peptide Bond: φ Bond & ψ Bond11:22
- Secondary Structure15:08
- α-Helix Folding Pattern17:28
- Illustration 1: α-Helix Folding Pattern19:22
- Illustration 2: α-Helix Folding Pattern21:39
- β-Sheet25:16
- β-Conformation26:04
- Parallel & Anti-parallel28:44
- Parallel β-Conformation Arrangement of the Peptide Chain30:12
- Putting Together a Parallel Peptide Chain35:16
- Anti-Parallel β-Conformation Arrangement37:42
- Tertiary Structure45:03
- Quaternary Structure45:52
- Illustration 3: Myoglobin Tertiary Structure & Hemoglobin Quaternary Structure47:13
- Final Words on Alpha Helix and Beta Conformation48:34
51m 36s
- Intro0:00
- Protein Function I: Ligand Binding & Myoglobin0:30
- Ligand1:02
- Binding Site2:06
- Proteins are Not Static or Fixed3:36
- Multi-Subunit Proteins5:46
- O₂ as a Ligand7:21
- Myoglobin, Protoporphyrin IX, Fe ²⁺, and O₂12:54
- Protoporphyrin Illustration14:25
- Myoglobin With a Heme Group Illustration17:02
- Fe²⁺ has 6 Coordination Sites & Binds O₂18:10
- Heme19:44
- Myoglobin Overview22:40
- Myoglobin and O₂ Interaction23:34
- Keq or Ka & The Measure of Protein's Affinity for Its Ligand26:46
- Defining α: Fraction of Binding Sites Occupied32:52
- Graph: α vs. [L]37:33
- For The Special Case of α = 0.539:01
- Association Constant & Dissociation Constant43:54
- α & Kd45:15
- Myoglobin's Binding of O₂48:20
1h 3m 36s
- Intro0:00
- Protein Function II: Hemoglobin0:14
- Hemoglobin Overview0:15
- Hemoglobin & Its 4 Subunits1:22
- α and β Interactions5:18
- Two Major Conformations of Hb: T State (Tense) & R State (Relaxed)8:06
- Transition From The T State to R State12:03
- Binding of Hemoglobins & O₂14:02
- Binding Curve18:32
- Hemoglobin in the Lung27:28
- Signoid Curve30:13
- Cooperative Binding32:25
- Hemoglobin is an Allosteric Protein34:26
- Homotropic Allostery36:18
- Describing Cooperative Binding Quantitatively38:06
- Deriving The Hill Equation41:52
- Graphing the Hill Equation44:43
- The Slope and Degree of Cooperation46:25
- The Hill Coefficient49:48
- Hill Coefficient = 151:08
- Hill Coefficient < 155:55
- Where the Graph Hits the x-axis56:11
- Graph for Hemoglobin58:02
1h 7m 16s
- Intro0:00
- Protein Function III: More on Hemoglobin0:11
- Two Models for Cooperative Binding: MWC & Sequential Model0:12
- MWC Model1:31
- Hemoglobin Subunits3:32
- Sequential Model8:00
- Hemoglobin Transports H⁺ & CO₂17:23
- Binding Sites of H⁺ and CO₂19:36
- CO₂ is Converted to Bicarbonate23:28
- Production of H⁺ & CO₂ in Tissues27:28
- H⁺ & CO₂ Binding are Inversely Related to O₂ Binding28:31
- The H⁺ Bohr Effect: His¹⁴⁶ Residue on the β Subunits33:31
- Heterotropic Allosteric Regulation of O₂ Binding by 2,3-Biphosphoglycerate (2,3 BPG)39:53
- Binding Curve for 2,3 BPG56:21
41m 38s
- Intro0:00
- Enzymes I0:38
- Enzymes Overview0:39
- Cofactor4:38
- Holoenzyme5:52
- Apoenzyme6:40
- Riboflavin, FAD, Pyridoxine, Pyridoxal Phosphate Structures7:28
- Carbonic Anhydrase8:45
- Classification of Enzymes9:55
- Example: EC 1.1.1.113:04
- Reaction of Oxidoreductases16:23
- Enzymes: Catalysts, Active Site, and Substrate18:28
- Illustration of Enzymes, Substrate, and Active Site27:22
- Catalysts & Activation Energies29:57
- Intermediates36:00
44m 2s
- Intro0:00
- Enzymes II: Transitions State, Binding Energy, & Induced Fit0:18
- Enzymes 'Fitting' Well With The Transition State0:20
- Example Reaction: Breaking of a Stick3:40
- Another Energy Diagram8:20
- Binding Energy9:48
- Enzymes Specificity11:03
- Key Point: Optimal Interactions Between Substrate & Enzymes15:15
- Induced Fit16:25
- Illustrations: Induced Fit20:58
- Enzymes II: Catalytic Mechanisms22:17
- General Acid/Base Catalysis23:56
- Acid Form & Base Form of Amino Acid: Glu &Asp25:26
- Acid Form & Base Form of Amino Acid: Lys & Arg26:30
- Acid Form & Base Form of Amino Acid: Cys26:51
- Acid Form & Base Form of Amino Acid: His27:30
- Acid Form & Base Form of Amino Acid: Ser28:16
- Acid Form & Base Form of Amino Acid: Tyr28:30
- Example: Phosphohexose Isomerase29:20
- Covalent Catalysis34:19
- Example: Glyceraldehyde 3-Phosphate Dehydrogenase35:34
- Metal Ion Catalysis: Isocitrate Dehydrogenase38:45
- Function of Mn²⁺42:15
56m 40s
- Intro0:00
- Enzymes III: Kinetics1:40
- Rate of an Enzyme-Catalyzed Reaction & Substrate Concentration1:41
- Graph: Substrate Concentration vs. Reaction Rate10:43
- Rate At Low and High Substrate Concentration14:26
- Michaelis & Menten Kinetics20:16
- More On Rate & Concentration of Substrate22:46
- Steady-State Assumption26:02
- Rate is Determined by How Fast ES Breaks Down to Product31:36
- Total Enzyme Concentration: [Et] = [E] + [ES]35:35
- Rate of ES Formation36:44
- Rate of ES Breakdown38:40
- Measuring Concentration of Enzyme-Substrate Complex41:19
- Measuring Initial & Maximum Velocity43:43
- Michaelis & Menten Equation46:44
- What Happens When V₀ = (1/2) Vmax?49:12
- When [S] << Km53:32
- When [S] >> Km54:44
20m 37s
- Intro0:00
- Enzymes IV: Lineweaver-Burk Plots0:45
- Deriving The Lineweaver-Burk Equation0:46
- Lineweaver-Burk Plots3:55
- Example 1: Carboxypeptidase A8:00
- More on Km, Vmax, and Enzyme-catalyzed Reaction15:54
51m 37s
- Intro0:00
- Enzymes V: Enzyme Inhibition Overview0:42
- Enzyme Inhibitors Overview0:43
- Classes of Inhibitors2:32
- Competitive Inhibition3:08
- Competitive Inhibition3:09
- Michaelis & Menten Equation in the Presence of a Competitive Inhibitor7:40
- Double-Reciprocal Version of the Michaelis & Menten Equation14:48
- Competitive Inhibition Graph16:37
- Uncompetitive Inhibition19:23
- Uncompetitive Inhibitor19:24
- Michaelis & Menten Equation for Uncompetitive Inhibition22:10
- The Lineweaver-Burk Equation for Uncompetitive Inhibition26:04
- Uncompetitive Inhibition Graph27:42
- Mixed Inhibition30:30
- Mixed Inhibitor30:31
- Double-Reciprocal Version of the Equation33:34
- The Lineweaver-Burk Plots for Mixed Inhibition35:02
- Summary of Reversible Inhibitor Behavior38:00
- Summary of Reversible Inhibitor Behavior38:01
- Note: Non-Competitive Inhibition42:22
- Irreversible Inhibition45:15
- Irreversible Inhibition45:16
- Penicillin & Transpeptidase Enzyme46:50
51m 23s
- Intro0:00
- Enzymes VI: Regulatory Enzymes0:45
- Regulatory Enzymes Overview0:46
- Example: Glycolysis2:27
- Allosteric Regulatory Enzyme9:19
- Covalent Modification13:08
- Two Other Regulatory Processes16:28
- Allosteric Regulation20:58
- Feedback Inhibition25:12
- Feedback Inhibition Example: L-Threonine → L-Isoleucine26:03
- Covalent Modification27:26
- Covalent Modulators: -PO₃²⁻29:30
- Protein Kinases31:59
- Protein Phosphatases32:47
- Addition/Removal of -PO₃²⁻ and the Effect on Regulatory Enzyme33:36
- Phosphorylation Sites of a Regulatory Enzyme38:38
- Proteolytic Cleavage41:48
- Zymogens: Chymotrypsin & Trypsin43:58
- Enzymes That Use More Than One Regulatory Process: Bacterial Glutamine Synthetase48:59
- Why The Complexity?50:27
54m 49s
- Intro0:00
- Km1:48
- Recall the Michaelis–Menten Equation1:49
- Km & Enzyme's Affinity6:18
- Rate Forward, Rate Backward, and Equilibrium Constant11:08
- When an Enzyme's Affinity for Its Substrate is High14:17
- More on Km & Enzyme Affinity17:29
- The Measure of Km Under Michaelis–Menten kinetic23:19
- Kcat (First-order Rate Constant or Catalytic Rate Constant)24:10
- Kcat: Definition24:11
- Kcat & The Michaelis–Menten Postulate25:18
- Finding Vmax and [Et}27:27
- Units for Vmax and Kcat28:26
- Kcat: Turnover Number28:55
- Michaelis–Menten Equation32:12
- Km & Kcat36:37
- Second Order Rate Equation36:38
- (Kcat)/(Km): Overview39:22
- High (Kcat)/(Km)40:20
- Low (Kcat)/(Km)43:16
- Practical Big Picture46:28
- Upper Limit to (Kcat)/(Km)48:56
- More On Kcat and Km49:26
1h 17m 46s
- Intro0:00
- Monosaccharides1:49
- Carbohydrates Overview1:50
- Three Major Classes of Carbohydrates4:48
- Definition of Monosaccharides5:46
- Examples of Monosaccharides: Aldoses7:06
- D-Glyceraldehyde7:39
- D-Erythrose9:00
- D-Ribose10:10
- D-Glucose11:20
- Observation: Aldehyde Group11:54
- Observation: Carbonyl 'C'12:30
- Observation: D & L Naming System12:54
- Examples of Monosaccharides: Ketose16:54
- Dihydroxy Acetone17:28
- D-Erythrulose18:30
- D-Ribulose19:49
- D-Fructose21:10
- D-Glucose Comparison23:18
- More information of Ketoses24:50
- Let's Look Closer at D-Glucoses25:50
- Let's Look At All the D-Hexose Stereoisomers31:22
- D-Allose32:20
- D-Altrose33:01
- D-Glucose33:39
- D-Gulose35:00
- D-Mannose35:40
- D-Idose36:42
- D-Galactose37:14
- D-Talose37:42
- Epimer40:05
- Definition of Epimer40:06
- Example of Epimer: D-Glucose, D-Mannose, and D-Galactose40:57
- Hemiacetal or Hemiketal44:36
- Hemiacetal/Hemiketal Overview45:00
- Ring Formation of the α and β Configurations of D-Glucose50:52
- Ring Formation of the α and β Configurations of Fructose1:01:39
- Haworth Projection1:07:34
- Pyranose & Furanose Overview1:07:38
- Haworth Projection: Pyranoses1:09:30
- Haworth Projection: Furanose1:14:56
37m 6s
- Intro0:00
- Hexose Derivatives0:15
- Point of Clarification: Forming a Cyclic Sugar From a Linear Sugar0:16
- Let's Recall the α and β Anomers of Glucose8:42
- α-Glucose10:54
- Hexose Derivatives that Play Key Roles in Physiology Progression17:38
- β-Glucose18:24
- β-Glucosamine18:48
- N-Acetyl-β-Glucosamine20:14
- β-Glucose-6-Phosphate22:22
- D-Gluconate24:10
- Glucono-δ-Lactone26:33
- Reducing Sugars29:50
- Reducing Sugars Overview29:51
- Reducing Sugars Example: β-Galactose32:36
43m 32s
- Intro0:00
- Disaccharides0:15
- Disaccharides Overview0:19
- Examples of Disaccharides & How to Name Them2:49
- Disaccharides Trehalose Overview15:46
- Disaccharides Trehalose: Flip20:52
- Disaccharides Trehalose: Spin28:36
- Example: Draw the Structure33:12
39m 25s
- Intro0:00
- Recap Example: Draw the Structure of Gal(α1↔β1)Man0:38
- Polysaccharides9:46
- Polysaccharides Overview9:50
- Homopolysaccharide13:12
- Heteropolysaccharide13:47
- Homopolysaccharide as Fuel Storage16:23
- Starch Has Two Types of Glucose Polymer: Amylose17:10
- Starch Has Two Types of Glucose Polymer: Amylopectin18:04
- Polysaccharides: Reducing End & Non-Reducing End19:30
- Glycogen20:06
- Examples: Structures of Polysaccharides21:42
- Let's Draw an (α1→4) & (α1→6) of Amylopectin by Hand.28:14
- More on Glycogen31:17
- Glycogen, Concentration, & The Concept of Osmolarity35:16
44m 15s
- Intro0:00
- Polysaccharides0:17
- Example: Cellulose0:34
- Glycoside Bond7:25
- Example Illustrations12:30
- Glycosaminoglycans Part 115:55
- Glycosaminoglycans Part 218:34
- Glycosaminoglycans & Sulfate Attachments22:42
- β-D-N-Acetylglucosamine24:49
- β-D-N-AcetylGalactosamine25:42
- β-D-Glucuronate26:44
- β-L-Iduronate27:54
- More on Sulfate Attachments29:49
- Hylarunic Acid32:00
- Hyaluronates39:32
- Other Glycosaminoglycans40:46
44m 23s
- Intro0:00
- Glycoconjugates0:24
- Overview0:25
- Proteoglycan2:53
- Glycoprotein5:20
- Glycolipid7:25
- Proteoglycan vs. Glycoprotein8:15
- Cell Surface Diagram11:17
- Proteoglycan Common Structure14:24
- Example: Chondroitin-4-Sulfate15:06
- Glycoproteins19:50
- The Monomers that Commonly Show Up in The Oligo Portions of Glycoproteins28:02
- N-Acetylneuraminic Acid31:17
- L-Furose32:37
- Example of an N-Linked Oligosaccharide33:21
- Cell Membrane Structure36:35
- Glycolipids & Lipopolysaccharide37:22
- Structure Example41:28
40m 22s
- Intro0:00
- Example 11:09
- Example 22:34
- Example 35:12
- Example 416:19
- Question16:20
- Solution17:25
- Example 524:18
- Question24:19
- Structure of 2,3-Di-O-Methylglucose26:47
- Part A28:11
- Part B33:46
54m 55s
- Intro0:00
- Fatty Acids0:32
- Lipids Overview0:34
- Introduction to Fatty Acid3:18
- Saturated Fatty Acid6:13
- Unsaturated or Polyunsaturated Fatty Acid7:07
- Saturated Fatty Acid Example7:46
- Unsaturated Fatty Acid Example9:06
- Notation Example: Chain Length, Degree of Unsaturation, & Double Bonds Location of Fatty Acid11:56
- Example 1: Draw the Structure16:18
- Example 2: Give the Shorthand for cis,cis-5,8-Hexadecadienoic Acid20:12
- Example 323:12
- Solubility of Fatty Acids25:45
- Melting Points of Fatty Acids29:40
- Triacylglycerols34:13
- Definition of Triacylglycerols34:14
- Structure of Triacylglycerols35:08
- Example: Triacylglycerols40:23
- Recall Ester Formation43:57
- The Body's Primary Fuel-Reserves47:22
- Two Primary Advantages to Storing Energy as Triacylglycerols Instead of Glycogen: Number 149:24
- Two Primary Advantages to Storing Energy as Triacylglycerols Instead of Glycogen: Number 251:54
38m 51s
- Intro0:00
- Membrane Lipids0:26
- Definition of Membrane Lipids0:27
- Five Major Classes of Membrane Lipids2:38
- Glycerophospholipids5:04
- Glycerophospholipids Overview5:05
- The X Group8:05
- Example: Phosphatidyl Ethanolamine10:51
- Example: Phosphatidyl Choline13:34
- Phosphatidyl Serine15:16
- Head Groups16:50
- Ether Linkages Instead of Ester Linkages20:05
- Galactolipids23:39
- Galactolipids Overview23:40
- Monogalactosyldiacylglycerol: MGDG25:17
- Digalactosyldiacylglycerol: DGDG28:13
- Structure Examples 1: Lipid Bilayer31:35
- Structure Examples 2: Cross Section of a Cell34:56
- Structure Examples 3: MGDG & DGDG36:28
38m 20s
- Intro0:00
- Sphingolipids0:11
- Sphingolipid Overview0:12
- Sphingosine Structure1:42
- Ceramide3:56
- Subclasses of Sphingolipids Overview6:00
- Subclasses of Sphingolipids: Sphingomyelins7:53
- Sphingomyelins7:54
- Subclasses of Sphingolipids: Glycosphingolipid12:47
- Glycosphingolipid Overview12:48
- Cerebrosides & Globosides Overview14:33
- Example: Cerebrosides15:43
- Example: Globosides17:14
- Subclasses of Sphingolipids: Gangliosides19:07
- Gangliosides19:08
- Medical Application: Tay-Sachs Disease23:34
- Sterols30:45
- Sterols: Basic Structure30:46
- Important Example: Cholesterol32:01
- Structures Example34:13
48m 36s
- Intro0:00
- The Biologically Active Lipids0:44
- Phosphatidyl Inositol Structure0:45
- Phosphatidyl Inositol Reaction3:24
- Image Example12:49
- Eicosanoids14:12
- Arachidonic Acid & Membrane Lipid Containing Arachidonic Acid18:41
- Three Classes of Eicosanoids20:42
- Overall Structures21:38
- Prostagladins22:56
- Thromboxane27:19
- Leukotrienes30:19
- More On The Biologically Active Lipids33:34
- Steroid Hormones33:35
- Fat Soluble Vitamins38:25
- Vitamin D₃40:40
- Vitamin A43:17
- Vitamin E45:12
- Vitamin K47:17
45m 51s
- Intro0:00
- Thermodynamics, Free Energy and Equilibrium1:03
- Reaction: Glucose + Pi → Glucose 6-Phosphate1:50
- Thermodynamics & Spontaneous Processes3:31
- In Going From Reactants → Product, a Reaction Wants to Release Heat6:30
- A Reaction Wants to Become More Disordered9:10
- ∆H < 010:30
- ∆H > 010:57
- ∆S > 011:23
- ∆S <011:56
- ∆G = ∆H - T∆S at Constant Pressure12:15
- Gibbs Free Energy15:00
- ∆G < 016:49
- ∆G > 017:07
- Reference Frame For Thermodynamics Measurements17:57
- More On BioChemistry Standard22:36
- Spontaneity25:36
- Keq31:45
- Example: Glucose + Pi → Glucose 6-Phosphate34:14
- Example Problem 140:25
- Question40:26
- Solution41:12
37m 6s
- Intro0:00
- More on Thermodynamics & Free Energy0:16
- Calculating ∆G Under Standard Conditions0:17
- Calculating ∆G Under Physiological Conditions2:05
- ∆G < 05:39
- ∆G = 07:03
- Reaction Moving Forward Spontaneously8:00
- ∆G & The Maximum Theoretical Amount of Free Energy Available10:36
- Example Problem 113:11
- Reactions That Have Species in Common17:48
- Example Problem 2: Part 120:10
- Example Problem 2: Part 2- Enzyme Hexokinase & Coupling25:08
- Example Problem 2: Part 330:34
- Recap34:45
44m 32s
- Intro0:00
- ATP & Other High-Energy Compounds0:10
- Endergonic Reaction Coupled With Exergonic Reaction0:11
- Major Theme In Metabolism6:56
- Why the ∆G°' for ATP Hydrolysis is Large & Negative12:24
- ∆G°' for ATP Hydrolysis12:25
- Reason 1: Electrostatic Repulsion14:24
- Reason 2: Pi & Resonance Forms15:33
- Reason 3: Concentrations of ADP & Pi17:32
- ATP & Other High-Energy Compounds Cont'd18:48
- More On ∆G°' & Hydrolysis18:49
- Other Compounds That Have Large Negative ∆G°' of Hydrolysis: Phosphoenol Pyruvate (PEP)25:14
- Enzyme Pyruvate Kinase30:36
- Another High Energy Molecule: 1,3 Biphosphoglycerate36:17
- Another High Energy Molecule: Phophocreatine39:41
30m 8s
- Intro0:00
- Phosphoryl Group Transfer0:27
- Phosphoryl Group Transfer Overview0:28
- Example: Glutamate → Glutamine Part 17:11
- Example: Glutamate → Glutamine Part 213:29
- ATP Not Only Transfers Phosphoryl, But Also Pyrophosphoryl & Adenylyl Groups17:03
- Attack At The γ Phosphorous Transfers a Phosphoryl19:02
- Attack At The β Phosphorous Gives Pyrophosphoryl22:44
49m 46s
- Intro0:00
- Oxidation-Reduction Reactions1:32
- Redox Reactions1:33
- Example 1: Mg + Al³⁺ → Mg²⁺ + Al3:49
- Reduction Potential Definition10:47
- Reduction Potential Example13:38
- Organic Example22:23
- Review: How To Find The Oxidation States For Carbon24:15
- Examples: Oxidation States For Carbon27:45
- Example 1: Oxidation States For Carbon27:46
- Example 2: Oxidation States For Carbon28:36
- Example 3: Oxidation States For Carbon29:18
- Example 4: Oxidation States For Carbon29:44
- Example 5: Oxidation States For Carbon30:10
- Example 6: Oxidation States For Carbon30:40
- Example 7: Oxidation States For Carbon31:20
- Example 8: Oxidation States For Carbon32:10
- Example 9: Oxidation States For Carbon32:52
- Oxidation-Reduction Reactions, cont'd35:22
- More On Reduction Potential35:28
- Lets' Start With ∆G = ∆G°' + RTlnQ38:29
- Example: Oxidation Reduction Reactions41:42
56m 34s
- Intro0:00
- More On Oxidation-Reduction Reactions0:10
- Example 1: What If the Concentrations Are Not Standard?0:11
- Alternate Procedure That Uses The 1/2 Reactions Individually8:57
- Universal Electron Carriers in Aqueous Medium: NAD+ & NADH15:12
- The Others Are…19:22
- NAD+ & NADP Coenzymes20:56
- FMN & FAD22:03
- Nicotinamide Adenine Dinucleotide (Phosphate)23:03
- Reduction 1/2 Reactions36:10
- Ratio of NAD+ : NADH36:52
- Ratio of NADPH : NADP+38:02
- Specialized Roles of NAD+ & NADPH38:48
- Oxidoreductase Enzyme Overview40:26
- Examples of Oxidoreductase43:32
- The Flavin Nucleotides46:46
42m 12s
- Intro0:00
- Example 1: Calculate the ∆G°' For The Following Reaction1:04
- Example 1: Question1:05
- Example 1: Solution2:20
- Example 2: Calculate the Keq For the Following4:20
- Example 2: Question4:21
- Example 2: Solution5:54
- Example 3: Calculate the ∆G°' For The Hydrolysis of ATP At 25°C8:52
- Example 3: Question8:53
- Example 3: Solution10:30
- Example 3: Alternate Procedure13:48
- Example 4: Problems For Bioenergetics16:46
- Example 4: Questions16:47
- Example 4: Part A Solution21:19
- Example 4: Part B Solution23:26
- Example 4: Part C Solution26:12
- Example 5: Problems For Bioenergetics29:27
- Example 5: Questions29:35
- Example 5: Solution - Part 132:16
- Example 5: Solution - Part 234:39
43m 32s
- Intro0:00
- Overview of Glycolysis0:48
- Three Primary Paths For Glucose1:04
- Preparatory Phase of Glycolysis4:40
- Payoff Phase of Glycolysis6:40
- Glycolysis Reactions Diagram7:58
- Enzymes of Glycolysis12:41
- Glycolysis Reactions16:02
- Step 116:03
- Step 218:03
- Step 318:52
- Step 420:08
- Step 521:42
- Step 622:44
- Step 724:22
- Step 825:11
- Step 926:00
- Step 1026:51
- Overview of Glycolysis Cont.27:28
- The Overall Reaction for Glycolysis27:29
- Recall The High-Energy Phosphorylated Compounds Discusses In The Bioenergetics Unit33:10
- What Happens To The Pyruvate That Is Formed?37:58
1h 1m 47s
- Intro0:00
- Glycolysis Step 1: The Phosphorylation of Glucose0:27
- Glycolysis Step 1: Reaction0:28
- Hexokinase2:28
- Glycolysis Step 1: Mechanism-Simple Nucleophilic Substitution6:34
- Glycolysis Step 2: Conversion of Glucose 6-Phosphate → Fructose 6-Phosphate11:33
- Glycolysis Step 2: Reaction11:34
- Glycolysis Step 2: Mechanism, Part 114:40
- Glycolysis Step 2: Mechanism, Part 218:16
- Glycolysis Step 2: Mechanism, Part 319:56
- Glycolysis Step 2: Mechanism, Part 4 (Ring Closing & Dissociation)21:54
- Glycolysis Step 3: Conversion of Fructose 6-Phosphate to Fructose 1,6-Biphosphate24:16
- Glycolysis Step 3: Reaction24:17
- Glycolysis Step 3: Mechanism26:40
- Glycolysis Step 4: Cleavage of Fructose 1,6-Biphosphate31:10
- Glycolysis Step 4: Reaction31:11
- Glycolysis Step 4: Mechanism, Part 1 (Binding & Ring Opening)35:26
- Glycolysis Step 4: Mechanism, Part 237:40
- Glycolysis Step 4: Mechanism, Part 339:30
- Glycolysis Step 4: Mechanism, Part 444:00
- Glycolysis Step 4: Mechanism, Part 546:34
- Glycolysis Step 4: Mechanism, Part 649:00
- Glycolysis Step 4: Mechanism, Part 750:12
- Hydrolysis of The Imine52:33
- Glycolysis Step 5: Conversion of Dihydroxyaceton Phosphate to Glyceraldehyde 3-Phosphate55:38
- Glycolysis Step 5: Reaction55:39
- Breakdown and Numbering of Sugar57:40
59m 17s
- Intro0:00
- Glycolysis Step 5: Conversion of Dihydroxyaceton Phosphate to Glyceraldehyde 3-Phosphate0:44
- Glycolysis Step 5: Mechanism, Part 10:45
- Glycolysis Step 5: Mechanism, Part 23:53
- Glycolysis Step 6: Oxidation of Glyceraldehyde 3-Phosphate to 1,3-Biphosphoglycerate5:14
- Glycolysis Step 6: Reaction5:15
- Glycolysis Step 6: Mechanism, Part 18:52
- Glycolysis Step 6: Mechanism, Part 212:58
- Glycolysis Step 6: Mechanism, Part 314:26
- Glycolysis Step 6: Mechanism, Part 416:23
- Glycolysis Step 7: Phosphoryl Transfer From 1,3-Biphosphoglycerate to ADP to Form ATP19:08
- Glycolysis Step 7: Reaction19:09
- Substrate-Level Phosphorylation23:18
- Glycolysis Step 7: Mechanism (Nucleophilic Substitution)26:57
- Glycolysis Step 8: Conversion of 3-Phosphoglycerate to 2-Phosphoglycerate28:44
- Glycolysis Step 8: Reaction28:45
- Glycolysis Step 8: Mechanism, Part 130:08
- Glycolysis Step 8: Mechanism, Part 232:24
- Glycolysis Step 8: Mechanism, Part 334:02
- Catalytic Cycle35:42
- Glycolysis Step 9: Dehydration of 2-Phosphoglycerate to Phosphoenol Pyruvate37:20
- Glycolysis Step 9: Reaction37:21
- Glycolysis Step 9: Mechanism, Part 140:12
- Glycolysis Step 9: Mechanism, Part 242:01
- Glycolysis Step 9: Mechanism, Part 343:58
- Glycolysis Step 10: Transfer of a Phosphoryl Group From Phosphoenol Pyruvate To ADP To Form ATP45:16
- Glycolysis Step 10: Reaction45:17
- Substrate-Level Phosphorylation48:32
- Energy Coupling Reaction51:24
- Glycolysis Balance Sheet54:15
- Glycolysis Balance Sheet54:16
- What Happens to The 6 Carbons of Glucose?56:22
- What Happens to 2 ADP & 2 Pi?57:04
- What Happens to The 4e⁻ ?57:15
39m 47s
- Intro0:00
- Feeder Pathways0:42
- Feeder Pathways Overview0:43
- Starch, Glycogen2:25
- Lactose4:38
- Galactose4:58
- Manose5:22
- Trehalose5:45
- Sucrose5:56
- Fructose6:07
- Fates of Pyruvate: Aerobic & Anaerobic Conditions7:39
- Aerobic Conditions & Pyruvate7:40
- Anaerobic Fates of Pyruvate11:18
- Fates of Pyruvate: Lactate Acid Fermentation14:10
- Lactate Acid Fermentation14:11
- Fates of Pyruvate: Ethanol Fermentation19:01
- Ethanol Fermentation Reaction19:02
- TPP: Thiamine Pyrophosphate (Functions and Structure)23:10
- Ethanol Fermentation Mechanism, Part 127:53
- Ethanol Fermentation Mechanism, Part 229:06
- Ethanol Fermentation Mechanism, Part 331:15
- Ethanol Fermentation Mechanism, Part 432:44
- Ethanol Fermentation Mechanism, Part 534:33
- Ethanol Fermentation Mechanism, Part 635:48
41m 34s
- Intro0:00
- Gluconeogenesis, Part 11:02
- Gluconeogenesis Overview1:03
- 3 Glycolytic Reactions That Are Irreversible Under Physiological Conditions2:29
- Gluconeogenesis Reactions Overview6:17
- Reaction: Pyruvate to Oxaloacetate11:07
- Reaction: Oxaloacetate to Phosphoenolpyruvate (PEP)13:29
- First Pathway That Pyruvate Can Take to Become Phosphoenolpyruvate15:24
- Second Pathway That Pyruvate Can Take to Become Phosphoenolpyruvate21:00
- Transportation of Pyruvate From The Cytosol to The Mitochondria24:15
- Transportation Mechanism, Part 126:41
- Transportation Mechanism, Part 230:43
- Transportation Mechanism, Part 334:04
- Transportation Mechanism, Part 438:14
34m 18s
- Intro0:00
- Oxaloacetate → Phosphoenolpyruvate (PEP)0:35
- Mitochondrial Membrane Does Not Have a Transporter for Oxaloactate0:36
- Reaction: Oxaloacetate to Phosphoenolpyruvate (PEP)3:36
- Mechanism: Oxaloacetate to Phosphoenolpyruvate (PEP)4:48
- Overall Reaction: Pyruvate to Phosphoenolpyruvate7:01
- Recall The Two Pathways That Pyruvate Can Take to Become Phosphoenolpyruvate10:16
- NADH in Gluconeogenesis12:29
- Second Pathway: Lactate → Pyruvate18:22
- Cytosolic PEP Carboxykinase, Mitochondrial PEP Carboxykinase, & Isozymes18:23
- 2nd Bypass Reaction23:04
- 3rd Bypass Reaction24:01
- Overall Process25:17
- Other Feeder Pathways For Gluconeogenesis26:35
- Carbon Intermediates of The Citric Acid Cycle26:36
- Amino Acids & The Gluconeogenic Pathway29:45
- Glycolysis & Gluconeogenesis Are Reciprocally Regulated32:00
42m 52s
- Intro0:00
- The Pentose Phosphate Pathway Overview0:17
- The Major Fate of Glucose-6-Phosphate0:18
- The Pentose Phosphate Pathway (PPP) Overview1:00
- Oxidative Phase of The Pentose Phosphate Pathway4:33
- Oxidative Phase of The Pentose Phosphate Pathway: Reaction Overview4:34
- Ribose-5-Phosphate: Glutathione & Reductive Biosynthesis9:02
- Glucose-6-Phosphate to 6-Phosphogluconate12:48
- 6-Phosphogluconate to Ribulose-5-Phosphate15:39
- Ribulose-5-Phosphate to Ribose-5-Phosphate17:05
- Non-Oxidative Phase of The Pentose Phosphate Pathway19:55
- Non-Oxidative Phase of The Pentose Phosphate Pathway: Overview19:56
- General Transketolase Reaction29:03
- Transaldolase Reaction35:10
- Final Transketolase Reaction39:10
36m 10s
- Intro0:00
- Stages of Cellular Respiration0:23
- Stages of Cellular Respiration0:24
- From Pyruvate to Acetyl-CoA6:56
- From Pyruvate to Acetyl-CoA: Pyruvate Dehydrogenase Complex6:57
- Overall Reaction8:42
- Oxidative Decarboxylation11:54
- Pyruvate Dehydrogenase (PDH) & Enzymes15:30
- Pyruvate Dehydrogenase (PDH) Requires 5 Coenzymes17:15
- Molecule of CoEnzyme A18:52
- Thioesters20:56
- Lipoic Acid22:31
- Lipoate Is Attached To a Lysine Residue On E₂24:42
- Pyruvate Dehydrogenase Complex: Reactions26:36
- E1: Reaction 1 & 230:38
- E2: Reaction 331:58
- E3: Reaction 4 & 532:44
- Substrate Channeling34:17
49m 20s
- Intro0:00
- Citric Acid Cycle Reactions Overview0:26
- Citric Acid Cycle Reactions Overview: Part 10:27
- Citric Acid Cycle Reactions Overview: Part 27:03
- Things to Note10:58
- Citric Acid Cycle Reactions & Mechanism13:57
- Reaction 1: Formation of Citrate13:58
- Reaction 1: Mechanism19:01
- Reaction 2: Citrate to Cis Aconistate to Isocitrate28:50
- Reaction 3: Isocitrate to α-Ketoglutarate32:35
- Reaction 3: Two Isocitrate Dehydrogenase Enzymes36:24
- Reaction 3: Mechanism37:33
- Reaction 4: Oxidation of α-Ketoglutarate to Succinyl-CoA41:38
- Reaction 4: Notes46:34
44m 11s
- Intro0:00
- Citric Acid Cycle Reactions & Mechanism0:21
- Reaction 5: Succinyl-CoA to Succinate0:24
- Reaction 5: Reaction Sequence2:35
- Reaction 6: Oxidation of Succinate to Fumarate8:28
- Reaction 7: Fumarate to Malate10:17
- Reaction 8: Oxidation of L-Malate to Oxaloacetate14:15
- More On The Citric Acid Cycle17:17
- Energy from Oxidation17:18
- How Can We Transfer This NADH Into the Mitochondria27:10
- Citric Cycle is Amphibolic - Works In Both Anabolic & Catabolic Pathways32:06
- Biosynthetic Processes34:29
- Anaplerotic Reactions Overview37:26
- Anaplerotic: Reaction 141:42
48m 11s
- Intro0:00
- Introduction to Fatty Acid Catabolism0:21
- Introduction to Fatty Acid Catabolism0:22
- Vertebrate Cells Obtain Fatty Acids for Catabolism From 3 Sources2:16
- Diet: Part 14:00
- Diet: Part 25:35
- Diet: Part 36:20
- Diet: Part 46:47
- Diet: Part 510:18
- Diet: Part 610:54
- Diet: Part 712:04
- Diet: Part 812:26
- Fats Stored in Adipocytes Overview13:54
- Fats Stored in Adipocytes (Fat Cells): Part 116:13
- Fats Stored in Adipocytes (Fat Cells): Part 217:16
- Fats Stored in Adipocytes (Fat Cells): Part 319:42
- Fats Stored in Adipocytes (Fat Cells): Part 420:52
- Fats Stored in Adipocytes (Fat Cells): Part 522:56
- Mobilization of TAGs Stored in Fat Cells24:35
- Fatty Acid Oxidation28:29
- Fatty Acid Oxidation28:48
- 3 Reactions of the Carnitine Shuttle30:42
- Carnitine Shuttle & The Mitochondrial Matrix36:25
- CAT I43:58
- Carnitine Shuttle is the Rate-Limiting Steps46:24
45m 58s
- Intro0:00
- Fatty Acid Catabolism0:15
- Fatty Acid Oxidation Takes Place in 3 Stages0:16
- β-Oxidation2:05
- β-Oxidation Overview2:06
- Reaction 14:20
- Reaction 27:35
- Reaction 38:52
- Reaction 410:16
- β-Oxidation Reactions Discussion11:34
- Notes On β-Oxidation15:14
- Double Bond After The First Reaction15:15
- Reaction 1 is Catalyzed by 3 Isozymes of Acyl-CoA Dehydrogenase16:04
- Reaction 2 & The Addition of H₂O18:38
- After Reaction 419:24
- Production of ATP20:04
- β-Oxidation of Unsaturated Fatty Acid21:25
- β-Oxidation of Unsaturated Fatty Acid22:36
- β-Oxidation of Mono-Unsaturates24:49
- β-Oxidation of Mono-Unsaturates: Reaction 124:50
- β-Oxidation of Mono-Unsaturates: Reaction 228:43
- β-Oxidation of Mono-Unsaturates: Reaction 330:50
- β-Oxidation of Mono-Unsaturates: Reaction 431:06
- β-Oxidation of Polyunsaturates32:29
- β-Oxidation of Polyunsaturates: Part 132:30
- β-Oxidation of Polyunsaturates: Part 237:08
- β-Oxidation of Polyunsaturates: Part 340:25
33m 18s
- Intro0:00
- Fatty Acid Catabolism0:43
- Oxidation of Fatty Acids With an Odd Number of Carbons0:44
- β-oxidation in the Mitochondrion & Two Other Pathways9:08
- ω-oxidation10:37
- α-oxidation17:22
- Ketone Bodies19:08
- Two Fates of Acetyl-CoA Formed by β-Oxidation Overview19:09
- Ketone Bodies: Acetone20:42
- Ketone Bodies: Acetoacetate20:57
- Ketone Bodies: D-β-hydroxybutyrate21:25
- Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 122:05
- Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 226:59
- Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 330:52
40m 59s
- Intro0:00
- Overview of The Aminotransferase Reaction0:25
- Overview of The Aminotransferase Reaction0:26
- The Aminotransferase Reaction: Process 13:06
- The Aminotransferase Reaction: Process 26:46
- Alanine From Muscle Tissue10:54
- Bigger Picture of the Aminotransferase Reaction14:52
- Looking Closely at Process 119:04
- Pyridoxal Phosphate (PLP)24:32
- Pyridoxamine Phosphate25:29
- Pyridoxine (B6)26:38
- The Function of PLP27:12
- Mechanism Examples28:46
- Reverse Reaction: Glutamate to α-Ketoglutarate35:34
39m 18s
- Intro0:00
- Glutamine & Alanine: The Urea Cycle I0:45
- Excess Ammonia, Glutamate, and Glutamine0:46
- Glucose-Alanine Cycle9:54
- Introduction to the Urea Cycle20:56
- The Urea Cycle: Production of the Carbamoyl Phosphate22:59
- The Urea Cycle: Reaction & Mechanism Involving the Carbamoyl Phosphate Synthetase33:36
36m 21s
- Intro0:00
- Glutamine & Alanine: The Urea Cycle II0:14
- The Urea Cycle Overview0:34
- Reaction 1: Ornithine → Citrulline7:30
- Reaction 2: Citrulline → Citrullyl-AMP11:15
- Reaction 2': Citrullyl-AMP → Argininosuccinate15:25
- Reaction 3: Argininosuccinate → Arginine20:42
- Reaction 4: Arginine → Orthinine24:00
- Links Between the Citric Acid Cycle & the Urea Cycle27:47
- Aspartate-argininosuccinate Shunt32:36
47m 58s
- Intro0:00
- Amino Acid Catabolism0:10
- Common Amino Acids and 6 Major Products0:11
- Ketogenic Amino Acid1:52
- Glucogenic Amino Acid2:51
- Amino Acid Catabolism Diagram4:18
- Cofactors That Play a Role in Amino Acid Catabolism7:00
- Biotin8:42
- Tetrahydrofolate10:44
- S-Adenosylmethionine (AdoMet)12:46
- Tetrahydrobiopterin13:53
- S-Adenosylmethionine & Tetrahydrobiopterin Molecules14:41
- Catabolism of Phenylalanine18:30
- Reaction 1: Phenylalanine to Tyrosine18:31
- Reaction 2: Tyrosine to p-Hydroxyphenylpyruvate21:36
- Reaction 3: p-Hydroxyphenylpyruvate to Homogentisate23:50
- Reaction 4: Homogentisate to Maleylacetoacetate25:42
- Reaction 5: Maleylacetoacetate to Fumarylacetoacetate28:20
- Reaction 6: Fumarylacetoacetate to Fumarate & Succinyl-CoA29:51
- Reaction 7: Fate of Fumarate & Succinyl-CoA31:14
- Phenylalanine Hydroxylase33:33
- The Phenylalanine Hydroxylase Reaction33:34
- Mixed-Function Oxidases40:26
- When Phenylalanine Hydoxylase is Defective: Phenylketonuria (PKU)44:13
41m 11s
- Intro0:00
- Oxidative Phosphorylation0:54
- Oxidative Phosphorylation Overview0:55
- Mitochondrial Electron Transport Chain Diagram7:15
- Enzyme Complex I of the Electron Transport Chain12:27
- Enzyme Complex II of the Electron Transport Chain14:02
- Enzyme Complex III of the Electron Transport Chain14:34
- Enzyme Complex IV of the Electron Transport Chain15:30
- Complexes Diagram16:25
- Complex I18:25
- Complex I Overview18:26
- What is Ubiquinone or Coenzyme Q?20:02
- Coenzyme Q Transformation22:37
- Complex I Diagram24:47
- Fe-S Proteins26:42
- Transfer of H⁺29:42
- Complex II31:06
- Succinate Dehydrogenase31:07
- Complex II Diagram & Process32:54
- Other Substrates Pass Their e⁻ to Q: Glycerol 3-Phosphate37:31
- Other Substrates Pass Their e⁻ to Q: Fatty Acyl-CoA39:02
36m 27s
- Intro0:00
- Complex III0:19
- Complex III Overview0:20
- Complex III: Step 11:56
- Complex III: Step 26:14
- Complex IV8:42
- Complex IV: Cytochrome Oxidase8:43
- Oxidative Phosphorylation, cont'd17:18
- Oxidative Phosphorylation: Summary17:19
- Equation 119:13
- How Exergonic is the Reaction?21:03
- Potential Energy Represented by Transported H⁺27:24
- Free Energy Change for the Production of an Electrochemical Gradient Via an Ion Pump28:48
- Free Energy Change in Active Mitochondria32:02
For more information, please see full course syllabus of Biochemistry
Biochemistry Amino Acid Catabolism
There are around 20 common amino acids, but all of them break down to six major products that enter the citric acid cycle. These products are: alpha-ketoglutarate, succinyl-CoA, fumarate, oxaloacetate, pyruvate, and acetoacetyl-CoA (these become ketone bodies). Important cofactors which contribute a carbon group include biotin, tetrahydrofolate, s-adenosylmethionine (AdoMet), and tetrahydrobiopterin. In the example of the catabolism of phenylalanine, the amino acid undergoes seven steps: phenylalanine becomes tyrosine, which becomes p-hydroxyphenylpyruvate. That becomes homogentisate, which turns into maleylacetoacetate. Maleylacetoacetate converts to fumarylacetoacetate, which breaks down to fumarate and succinyl-CoA. Fumarate enters the citric acid cycle while acetoacetate becomes acetyl-CoA which can enter the citric acid cycle or form a ketone body in the liver. People with phenylketonuria cannot perform the first reaction, which can lead to a buildup of phenylpyruvate.
Share this knowledge with your friends!
Copy & Paste this embed code into your website’s HTML
Please ensure that your website editor is in text mode when you paste the code.(In Wordpress, the mode button is on the top right corner.)
- - Allow users to view the embedded video in full-size.
2 answers
Last reply by: Sally Reina
Thu Sep 7, 2017 2:07 PM
Post by Sally Reina on September 6, 2017
Hi Professor Raffi Hovasapian! Thanks for the helpful and well explained lecture :) !!
Isn't Threonine also both ketogenic and glucogenic? I was confused because my own biochemistry professor's powerpoint slides did not match up. In one slide it is glucogenic and in another it is both ketogenic and glucogenic. Then, I checked in a different biochemistry textbook were is it classified as both ketogenic and glucogenic.
Can you please confirm or clarify this for me?
Thanks so much :)!
1 answer
Last reply by: Professor Hovasapian
Tue Oct 29, 2013 5:35 PM
Post by Jennifer Parkinson on October 29, 2013
I can't tell you how much your lectures have helped me with my studies. I wish all lecturers explained things as well as you do! Thank you Professor H!