Raffi Hovasapian

Raffi Hovasapian

Overview of Glycolysis I

Slide Duration:

Table of Contents

Section 1: Preliminaries on Aqueous Chemistry
Aqueous Solutions & Concentration

39m 57s

Intro
0:00
Aqueous Solutions and Concentration
0:46
Definition of Solution
1:28
Example: Sugar Dissolved in Water
2:19
Example: Salt Dissolved in Water
3:04
A Solute Does Not Have to Be a Solid
3:37
A Solvent Does Not Have to Be a Liquid
5:02
Covalent Compounds
6:55
Ionic Compounds
7:39
Example: Table Sugar
9:12
Example: MgCl₂
10:40
Expressing Concentration: Molarity
13:42
Example 1
14:47
Example 1: Question
14:50
Example 1: Solution
15:40
Another Way to Express Concentration
22:01
Example 2
24:00
Example 2: Question
24:01
Example 2: Solution
24:49
Some Other Ways of Expressing Concentration
27:52
Example 3
29:30
Example 3: Question
29:31
Example 3: Solution
31:02
Dilution & Osmotic Pressure

38m 53s

Intro
0:00
Dilution
0:45
Definition of Dilution
0:46
Example 1: Question
2:08
Example 1: Basic Dilution Equation
4:20
Example 1: Solution
5:31
Example 2: Alternative Approach
12:05
Osmotic Pressure
14:34
Colligative Properties
15:02
Recall: Covalent Compounds and Soluble Ionic Compounds
17:24
Properties of Pure Water
19:42
Addition of a Solute
21:56
Osmotic Pressure: Conceptual Example
24:00
Equation for Osmotic Pressure
29:30
Example of 'i'
31:38
Example 3
32:50
More on Osmosis

29m 1s

Intro
0:00
More on Osmosis
1:25
Osmotic Pressure
1:26
Example 1: Molar Mass of Protein
5:25
Definition, Equation, and Unit of Osmolarity
13:13
Example 2: Osmolarity
15:19
Isotonic, Hypertonic, and Hypotonic
20:20
Example 3
22:20
More on Isotonic, Hypertonic, and Hypotonic
26:14
Osmosis vs. Osmotic Pressure
27:56
Acids & Bases

39m 11s

Intro
0:00
Acids and Bases
1:16
Let's Begin With H₂O
1:17
P-Scale
4:22
Example 1
6:39
pH
9:43
Strong Acids
11:10
Strong Bases
13:52
Weak Acids & Bases Overview
14:32
Weak Acids
15:49
Example 2: Phosphoric Acid
19:30
Weak Bases
24:50
Weak Base Produces Hydroxide Indirectly
25:41
Example 3: Pyridine
29:07
Acid Form and Base Form
32:02
Acid Reaction
35:50
Base Reaction
36:27
Ka, Kb, and Kw
37:14
Titrations and Buffers

41m 33s

Intro
0:00
Titrations
0:27
Weak Acid
0:28
Rearranging the Ka Equation
1:45
Henderson-Hasselbalch Equation
3:52
Fundamental Reaction of Acids and Bases
5:36
The Idea Behind a Titration
6:27
Let's Look at an Acetic Acid Solution
8:44
Titration Curve
17:00
Acetate
23:57
Buffers
26:57
Introduction to Buffers
26:58
What is a Buffer?
29:40
Titration Curve & Buffer Region
31:44
How a Buffer Works: Adding OH⁻
34:44
How a Buffer Works: Adding H⁺
35:58
Phosphate Buffer System
38:02
Example Problems with Acids, Bases & Buffers

44m 19s

Intro
0:00
Example 1
1:21
Example 1: Properties of Glycine
1:22
Example 1: Part A
3:40
Example 1: Part B
4:40
Example 2
9:02
Example 2: Question
9:03
Example 2: Total Phosphate Concentration
12:23
Example 2: Final Solution
17:10
Example 3
19:34
Example 3: Question
19:35
Example 3: pH Before
22:18
Example 3: pH After
24:24
Example 3: New pH
27:54
Example 4
30:00
Example 4: Question
30:01
Example 4: Equilibria
32:52
Example 4: 1st Reaction
38:04
Example 4: 2nd Reaction
39:53
Example 4: Final Solution
41:33
Hydrolysis & Condensation Reactions

18m 45s

Intro
0:00
Hydrolysis and Condensation Reactions
0:50
Hydrolysis
0:51
Condensation
2:42
Example 1: Hydrolysis of Ethyl Acetate
4:52
Example 2: Condensation of Acetic Acid with Ethanol
8:42
Example 3
11:18
Example 4: Formation & Hydrolysis of a Peptide Bond Between the Amino Acids Alanine & Serine
14:56
Section 2: Amino Acids & Proteins: Primary Structure
Amino Acids

38m 19s

Intro
0:00
Amino Acids
0:17
Proteins & Amino Acids
0:18
Difference Between Amino Acids
4:20
α-Carbon
7:08
Configuration in Biochemistry
10:43
L-Glyceraldehyde & Fischer Projection
12:32
D-Glyceraldehyde & Fischer Projection
15:31
Amino Acids in Biological Proteins are the L Enantiomer
16:50
L-Amino Acid
18:04
L-Amino Acids Correspond to S-Enantiomers in the RS System
20:10
Classification of Amino Acids
22:53
Amino Acids With Non-Polar R Groups
26:45
Glycine
27:00
Alanine
27:48
Valine
28:15
Leucine
28:58
Proline
31:08
Isoleucine
32:42
Methionine
33:43
Amino Acids With Aromatic R Groups
34:33
Phenylalanine
35:26
Tyrosine
36:02
Tryptophan
36:32
Amino Acids, Continued

27m 14s

Intro
0:00
Amino Acids With Positively Charged R Groups
0:16
Lysine
0:52
Arginine
1:55
Histidine
3:15
Amino Acids With Negatively Charged R Groups
6:28
Aspartate
6:58
Glutamate
8:11
Amino Acids With Uncharged, but Polar R Groups
8:50
Serine
8:51
Threonine
10:21
Cysteine
11:06
Asparagine
11:35
Glutamine
12:44
More on Amino Acids
14:18
Cysteine Dimerizes to Form Cystine
14:53
Tryptophan, Tyrosine, and Phenylalanine
19:07
Other Amino Acids
20:53
Other Amino Acids: Hydroxy Lysine
22:34
Other Amino Acids: r-Carboxy Glutamate
25:37
Acid/Base Behavior of Amino Acids

48m 28s

Intro
0:00
Acid/Base Behavior of Amino Acids
0:27
Acid/Base Behavior of Amino Acids
0:28
Let's Look at Alanine
1:57
Titration of Acidic Solution of Alanine with a Strong Base
2:51
Amphoteric Amino Acids
13:24
Zwitterion & Isoelectric Point
16:42
Some Amino Acids Have 3 Ionizable Groups
20:35
Example: Aspartate
24:44
Example: Tyrosine
28:50
Rule of Thumb
33:04
Basis for the Rule
35:59
Example: Describe the Degree of Protonation for Each Ionizable Group
38:46
Histidine is Special
44:58
Peptides & Proteins

45m 18s

Intro
0:00
Peptides and Proteins
0:15
Introduction to Peptides and Proteins
0:16
Formation of a Peptide Bond: The Bond Between 2 Amino Acids
1:44
Equilibrium
7:53
Example 1: Build the Following Tripeptide Ala-Tyr-Ile
9:48
Example 1: Shape Structure
15:43
Example 1: Line Structure
17:11
Peptides Bonds
20:08
Terms We'll Be Using Interchangeably
23:14
Biological Activity & Size of a Peptide
24:58
Multi-Subunit Proteins
30:08
Proteins and Prosthetic Groups
32:13
Carbonic Anhydrase
37:35
Primary, Secondary, Tertiary, and Quaternary Structure of Proteins
40:26
Amino Acid Sequencing of a Peptide Chain

42m 47s

Intro
0:00
Amino Acid Sequencing of a Peptide Chain
0:30
Amino Acid Sequence and Its Structure
0:31
Edman Degradation: Overview
2:57
Edman Degradation: Reaction - Part 1
4:58
Edman Degradation: Reaction - Part 2
10:28
Edman Degradation: Reaction - Part 3
13:51
Mechanism Step 1: PTC (Phenylthiocarbamyl) Formation
19:01
Mechanism Step 2: Ring Formation & Peptide Bond Cleavage
23:03
Example: Write Out the Edman Degradation for the Tripeptide Ala-Tyr-Ser
30:29
Step 1
30:30
Step 2
34:21
Step 3
36:56
Step 4
38:28
Step 5
39:24
Step 6
40:44
Sequencing Larger Peptides & Proteins

1h 2m 33s

Intro
0:00
Sequencing Larger Peptides and Proteins
0:28
Identifying the N-Terminal Amino Acids With the Reagent Fluorodinitrobenzene (FDNB)
0:29
Sequencing Longer Peptides & Proteins Overview
5:54
Breaking Peptide Bond: Proteases and Chemicals
8:16
Some Enzymes/Chemicals Used for Fragmentation: Trypsin
11:14
Some Enzymes/Chemicals Used for Fragmentation: Chymotrypsin
13:02
Some Enzymes/Chemicals Used for Fragmentation: Cyanogen Bromide
13:28
Some Enzymes/Chemicals Used for Fragmentation: Pepsin
13:44
Cleavage Location
14:04
Example: Chymotrypsin
16:44
Example: Pepsin
18:17
More on Sequencing Larger Peptides and Proteins
19:29
Breaking Disulfide Bonds: Performic Acid
26:08
Breaking Disulfide Bonds: Dithiothreitol Followed by Iodoacetate
31:04
Example: Sequencing Larger Peptides and Proteins
37:03
Part 1 - Breaking Disulfide Bonds, Hydrolysis and Separation
37:04
Part 2 - N-Terminal Identification
44:16
Part 3 - Sequencing Using Pepsin
46:43
Part 4 - Sequencing Using Cyanogen Bromide
52:02
Part 5 - Final Sequence
56:48
Peptide Synthesis (Merrifield Process)

49m 12s

Intro
0:00
Peptide Synthesis (Merrifield Process)
0:31
Introduction to Synthesizing Peptides
0:32
Merrifield Peptide Synthesis: General Scheme
3:03
So What Do We Do?
6:07
Synthesis of Protein in the Body Vs. The Merrifield Process
7:40
Example: Synthesis of Ala-Gly-Ser
9:21
Synthesis of Ala-Gly-Ser: Reactions Overview
11:41
Synthesis of Ala-Gly-Ser: Reaction 1
19:34
Synthesis of Ala-Gly-Ser: Reaction 2
24:34
Synthesis of Ala-Gly-Ser: Reaction 3
27:34
Synthesis of Ala-Gly-Ser: Reaction 4 & 4a
28:48
Synthesis of Ala-Gly-Ser: Reaction 5
33:38
Synthesis of Ala-Gly-Ser: Reaction 6
36:45
Synthesis of Ala-Gly-Ser: Reaction 7 & 7a
37:44
Synthesis of Ala-Gly-Ser: Reaction 8
39:47
Synthesis of Ala-Gly-Ser: Reaction 9 & 10
43:23
Chromatography: Eluent, Stationary Phase, and Eluate
45:55
More Examples with Amino Acids & Peptides

54m 31s

Intro
0:00
Example 1
0:22
Data
0:23
Part A: What is the pI of Serine & Draw the Correct Structure
2:11
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 Serine
10:50
Part D: Draw the Titration Curve for This Situation
14:50
Part E: The 10 mL of NaOH Added to the Solution at the pI is How Many Equivalents?
17:35
Part F: Serine Buffer Solution
20:22
Example 2
23:04
Data
23:05
Part A: Calculate the Minimum Molar Mass of the Protein
25:12
Part B: How Many Tyr Residues in this Protein?
28:34
Example 3
30:08
Question
30:09
Solution
34:30
Example 4
48:46
Question
48:47
Solution
49:50
Section 3: Proteins: Secondary, Tertiary, and Quaternary Structure
Alpha Helix & Beta Conformation

50m 52s

Intro
0:00
Alpha Helix and Beta Conformation
0:28
Protein Structure Overview
0:29
Weak interactions Among the Amino Acid in the Peptide Chain
2:11
Two Principals of Folding Patterns
4:56
Peptide Bond
7:00
Peptide Bond: Resonance
9:46
Peptide Bond: φ Bond & ψ Bond
11:22
Secondary Structure
15:08
α-Helix Folding Pattern
17:28
Illustration 1: α-Helix Folding Pattern
19:22
Illustration 2: α-Helix Folding Pattern
21:39
β-Sheet
25:16
β-Conformation
26:04
Parallel & Anti-parallel
28:44
Parallel β-Conformation Arrangement of the Peptide Chain
30:12
Putting Together a Parallel Peptide Chain
35:16
Anti-Parallel β-Conformation Arrangement
37:42
Tertiary Structure
45:03
Quaternary Structure
45:52
Illustration 3: Myoglobin Tertiary Structure & Hemoglobin Quaternary Structure
47:13
Final Words on Alpha Helix and Beta Conformation
48:34
Section 4: Proteins: Function
Protein Function I: Ligand Binding & Myoglobin

51m 36s

Intro
0:00
Protein Function I: Ligand Binding & Myoglobin
0:30
Ligand
1:02
Binding Site
2:06
Proteins are Not Static or Fixed
3:36
Multi-Subunit Proteins
5:46
O₂ as a Ligand
7:21
Myoglobin, Protoporphyrin IX, Fe ²⁺, and O₂
12:54
Protoporphyrin Illustration
14:25
Myoglobin With a Heme Group Illustration
17:02
Fe²⁺ has 6 Coordination Sites & Binds O₂
18:10
Heme
19:44
Myoglobin Overview
22:40
Myoglobin and O₂ Interaction
23:34
Keq or Ka & The Measure of Protein's Affinity for Its Ligand
26:46
Defining α: Fraction of Binding Sites Occupied
32:52
Graph: α vs. [L]
37:33
For The Special Case of α = 0.5
39:01
Association Constant & Dissociation Constant
43:54
α & Kd
45:15
Myoglobin's Binding of O₂
48:20
Protein Function II: Hemoglobin

1h 3m 36s

Intro
0:00
Protein Function II: Hemoglobin
0:14
Hemoglobin Overview
0:15
Hemoglobin & Its 4 Subunits
1:22
α and β Interactions
5:18
Two Major Conformations of Hb: T State (Tense) & R State (Relaxed)
8:06
Transition From The T State to R State
12:03
Binding of Hemoglobins & O₂
14:02
Binding Curve
18:32
Hemoglobin in the Lung
27:28
Signoid Curve
30:13
Cooperative Binding
32:25
Hemoglobin is an Allosteric Protein
34:26
Homotropic Allostery
36:18
Describing Cooperative Binding Quantitatively
38:06
Deriving The Hill Equation
41:52
Graphing the Hill Equation
44:43
The Slope and Degree of Cooperation
46:25
The Hill Coefficient
49:48
Hill Coefficient = 1
51:08
Hill Coefficient < 1
55:55
Where the Graph Hits the x-axis
56:11
Graph for Hemoglobin
58:02
Protein Function III: More on Hemoglobin

1h 7m 16s

Intro
0:00
Protein Function III: More on Hemoglobin
0:11
Two Models for Cooperative Binding: MWC & Sequential Model
0:12
MWC Model
1:31
Hemoglobin Subunits
3:32
Sequential Model
8:00
Hemoglobin Transports H⁺ & CO₂
17:23
Binding Sites of H⁺ and CO₂
19:36
CO₂ is Converted to Bicarbonate
23:28
Production of H⁺ & CO₂ in Tissues
27:28
H⁺ & CO₂ Binding are Inversely Related to O₂ Binding
28:31
The H⁺ Bohr Effect: His¹⁴⁶ Residue on the β Subunits
33:31
Heterotropic Allosteric Regulation of O₂ Binding by 2,3-Biphosphoglycerate (2,3 BPG)
39:53
Binding Curve for 2,3 BPG
56:21
Section 5: Enzymes
Enzymes I

41m 38s

Intro
0:00
Enzymes I
0:38
Enzymes Overview
0:39
Cofactor
4:38
Holoenzyme
5:52
Apoenzyme
6:40
Riboflavin, FAD, Pyridoxine, Pyridoxal Phosphate Structures
7:28
Carbonic Anhydrase
8:45
Classification of Enzymes
9:55
Example: EC 1.1.1.1
13:04
Reaction of Oxidoreductases
16:23
Enzymes: Catalysts, Active Site, and Substrate
18:28
Illustration of Enzymes, Substrate, and Active Site
27:22
Catalysts & Activation Energies
29:57
Intermediates
36:00
Enzymes II

44m 2s

Intro
0:00
Enzymes II: Transitions State, Binding Energy, & Induced Fit
0:18
Enzymes 'Fitting' Well With The Transition State
0:20
Example Reaction: Breaking of a Stick
3:40
Another Energy Diagram
8:20
Binding Energy
9:48
Enzymes Specificity
11:03
Key Point: Optimal Interactions Between Substrate & Enzymes
15:15
Induced Fit
16:25
Illustrations: Induced Fit
20:58
Enzymes II: Catalytic Mechanisms
22:17
General Acid/Base Catalysis
23:56
Acid Form & Base Form of Amino Acid: Glu &Asp
25:26
Acid Form & Base Form of Amino Acid: Lys & Arg
26:30
Acid Form & Base Form of Amino Acid: Cys
26:51
Acid Form & Base Form of Amino Acid: His
27:30
Acid Form & Base Form of Amino Acid: Ser
28:16
Acid Form & Base Form of Amino Acid: Tyr
28:30
Example: Phosphohexose Isomerase
29:20
Covalent Catalysis
34:19
Example: Glyceraldehyde 3-Phosphate Dehydrogenase
35:34
Metal Ion Catalysis: Isocitrate Dehydrogenase
38:45
Function of Mn²⁺
42:15
Enzymes III: Kinetics

56m 40s

Intro
0:00
Enzymes III: Kinetics
1:40
Rate of an Enzyme-Catalyzed Reaction & Substrate Concentration
1:41
Graph: Substrate Concentration vs. Reaction Rate
10:43
Rate At Low and High Substrate Concentration
14:26
Michaelis & Menten Kinetics
20:16
More On Rate & Concentration of Substrate
22:46
Steady-State Assumption
26:02
Rate is Determined by How Fast ES Breaks Down to Product
31:36
Total Enzyme Concentration: [Et] = [E] + [ES]
35:35
Rate of ES Formation
36:44
Rate of ES Breakdown
38:40
Measuring Concentration of Enzyme-Substrate Complex
41:19
Measuring Initial & Maximum Velocity
43:43
Michaelis & Menten Equation
46:44
What Happens When V₀ = (1/2) Vmax?
49:12
When [S] << Km
53:32
When [S] >> Km
54:44
Enzymes IV: Lineweaver-Burk Plots

20m 37s

Intro
0:00
Enzymes IV: Lineweaver-Burk Plots
0:45
Deriving The Lineweaver-Burk Equation
0:46
Lineweaver-Burk Plots
3:55
Example 1: Carboxypeptidase A
8:00
More on Km, Vmax, and Enzyme-catalyzed Reaction
15:54
Enzymes V: Enzyme Inhibition

51m 37s

Intro
0:00
Enzymes V: Enzyme Inhibition Overview
0:42
Enzyme Inhibitors Overview
0:43
Classes of Inhibitors
2:32
Competitive Inhibition
3:08
Competitive Inhibition
3:09
Michaelis & Menten Equation in the Presence of a Competitive Inhibitor
7:40
Double-Reciprocal Version of the Michaelis & Menten Equation
14:48
Competitive Inhibition Graph
16:37
Uncompetitive Inhibition
19:23
Uncompetitive Inhibitor
19:24
Michaelis & Menten Equation for Uncompetitive Inhibition
22:10
The Lineweaver-Burk Equation for Uncompetitive Inhibition
26:04
Uncompetitive Inhibition Graph
27:42
Mixed Inhibition
30:30
Mixed Inhibitor
30:31
Double-Reciprocal Version of the Equation
33:34
The Lineweaver-Burk Plots for Mixed Inhibition
35:02
Summary of Reversible Inhibitor Behavior
38:00
Summary of Reversible Inhibitor Behavior
38:01
Note: Non-Competitive Inhibition
42:22
Irreversible Inhibition
45:15
Irreversible Inhibition
45:16
Penicillin & Transpeptidase Enzyme
46:50
Enzymes VI: Regulatory Enzymes

51m 23s

Intro
0:00
Enzymes VI: Regulatory Enzymes
0:45
Regulatory Enzymes Overview
0:46
Example: Glycolysis
2:27
Allosteric Regulatory Enzyme
9:19
Covalent Modification
13:08
Two Other Regulatory Processes
16:28
Allosteric Regulation
20:58
Feedback Inhibition
25:12
Feedback Inhibition Example: L-Threonine → L-Isoleucine
26:03
Covalent Modification
27:26
Covalent Modulators: -PO₃²⁻
29:30
Protein Kinases
31:59
Protein Phosphatases
32:47
Addition/Removal of -PO₃²⁻ and the Effect on Regulatory Enzyme
33:36
Phosphorylation Sites of a Regulatory Enzyme
38:38
Proteolytic Cleavage
41:48
Zymogens: Chymotrypsin & Trypsin
43:58
Enzymes That Use More Than One Regulatory Process: Bacterial Glutamine Synthetase
48:59
Why The Complexity?
50:27
Enzymes VII: Km & Kcat

54m 49s

Intro
0:00
Km
1:48
Recall the Michaelis–Menten Equation
1:49
Km & Enzyme's Affinity
6:18
Rate Forward, Rate Backward, and Equilibrium Constant
11:08
When an Enzyme's Affinity for Its Substrate is High
14:17
More on Km & Enzyme Affinity
17:29
The Measure of Km Under Michaelis–Menten kinetic
23:19
Kcat (First-order Rate Constant or Catalytic Rate Constant)
24:10
Kcat: Definition
24:11
Kcat & The Michaelis–Menten Postulate
25:18
Finding Vmax and [Et}
27:27
Units for Vmax and Kcat
28:26
Kcat: Turnover Number
28:55
Michaelis–Menten Equation
32:12
Km & Kcat
36:37
Second Order Rate Equation
36:38
(Kcat)/(Km): Overview
39:22
High (Kcat)/(Km)
40:20
Low (Kcat)/(Km)
43:16
Practical Big Picture
46:28
Upper Limit to (Kcat)/(Km)
48:56
More On Kcat and Km
49:26
Section 6: Carbohydrates
Monosaccharides

1h 17m 46s

Intro
0:00
Monosaccharides
1:49
Carbohydrates Overview
1:50
Three Major Classes of Carbohydrates
4:48
Definition of Monosaccharides
5:46
Examples of Monosaccharides: Aldoses
7:06
D-Glyceraldehyde
7:39
D-Erythrose
9:00
D-Ribose
10:10
D-Glucose
11:20
Observation: Aldehyde Group
11:54
Observation: Carbonyl 'C'
12:30
Observation: D & L Naming System
12:54
Examples of Monosaccharides: Ketose
16:54
Dihydroxy Acetone
17:28
D-Erythrulose
18:30
D-Ribulose
19:49
D-Fructose
21:10
D-Glucose Comparison
23:18
More information of Ketoses
24:50
Let's Look Closer at D-Glucoses
25:50
Let's Look At All the D-Hexose Stereoisomers
31:22
D-Allose
32:20
D-Altrose
33:01
D-Glucose
33:39
D-Gulose
35:00
D-Mannose
35:40
D-Idose
36:42
D-Galactose
37:14
D-Talose
37:42
Epimer
40:05
Definition of Epimer
40:06
Example of Epimer: D-Glucose, D-Mannose, and D-Galactose
40:57
Hemiacetal or Hemiketal
44:36
Hemiacetal/Hemiketal Overview
45:00
Ring Formation of the α and β Configurations of D-Glucose
50:52
Ring Formation of the α and β Configurations of Fructose
1:01:39
Haworth Projection
1:07:34
Pyranose & Furanose Overview
1:07:38
Haworth Projection: Pyranoses
1:09:30
Haworth Projection: Furanose
1:14:56
Hexose Derivatives & Reducing Sugars

37m 6s

Intro
0:00
Hexose Derivatives
0:15
Point of Clarification: Forming a Cyclic Sugar From a Linear Sugar
0:16
Let's Recall the α and β Anomers of Glucose
8:42
α-Glucose
10:54
Hexose Derivatives that Play Key Roles in Physiology Progression
17:38
β-Glucose
18:24
β-Glucosamine
18:48
N-Acetyl-β-Glucosamine
20:14
β-Glucose-6-Phosphate
22:22
D-Gluconate
24:10
Glucono-δ-Lactone
26:33
Reducing Sugars
29:50
Reducing Sugars Overview
29:51
Reducing Sugars Example: β-Galactose
32:36
Disaccharides

43m 32s

Intro
0:00
Disaccharides
0:15
Disaccharides Overview
0:19
Examples of Disaccharides & How to Name Them
2:49
Disaccharides Trehalose Overview
15:46
Disaccharides Trehalose: Flip
20:52
Disaccharides Trehalose: Spin
28:36
Example: Draw the Structure
33:12
Polysaccharides

39m 25s

Intro
0:00
Recap Example: Draw the Structure of Gal(α1↔β1)Man
0:38
Polysaccharides
9:46
Polysaccharides Overview
9:50
Homopolysaccharide
13:12
Heteropolysaccharide
13:47
Homopolysaccharide as Fuel Storage
16:23
Starch Has Two Types of Glucose Polymer: Amylose
17:10
Starch Has Two Types of Glucose Polymer: Amylopectin
18:04
Polysaccharides: Reducing End & Non-Reducing End
19:30
Glycogen
20:06
Examples: Structures of Polysaccharides
21:42
Let's Draw an (α1→4) & (α1→6) of Amylopectin by Hand.
28:14
More on Glycogen
31:17
Glycogen, Concentration, & The Concept of Osmolarity
35:16
Polysaccharides, Part 2

44m 15s

Intro
0:00
Polysaccharides
0:17
Example: Cellulose
0:34
Glycoside Bond
7:25
Example Illustrations
12:30
Glycosaminoglycans Part 1
15:55
Glycosaminoglycans Part 2
18:34
Glycosaminoglycans & Sulfate Attachments
22:42
β-D-N-Acetylglucosamine
24:49
β-D-N-AcetylGalactosamine
25:42
β-D-Glucuronate
26:44
β-L-Iduronate
27:54
More on Sulfate Attachments
29:49
Hylarunic Acid
32:00
Hyaluronates
39:32
Other Glycosaminoglycans
40:46
Glycoconjugates

44m 23s

Intro
0:00
Glycoconjugates
0:24
Overview
0:25
Proteoglycan
2:53
Glycoprotein
5:20
Glycolipid
7:25
Proteoglycan vs. Glycoprotein
8:15
Cell Surface Diagram
11:17
Proteoglycan Common Structure
14:24
Example: Chondroitin-4-Sulfate
15:06
Glycoproteins
19:50
The Monomers that Commonly Show Up in The Oligo Portions of Glycoproteins
28:02
N-Acetylneuraminic Acid
31:17
L-Furose
32:37
Example of an N-Linked Oligosaccharide
33:21
Cell Membrane Structure
36:35
Glycolipids & Lipopolysaccharide
37:22
Structure Example
41:28
More Example Problems with Carbohydrates

40m 22s

Intro
0:00
Example 1
1:09
Example 2
2:34
Example 3
5:12
Example 4
16:19
Question
16:20
Solution
17:25
Example 5
24:18
Question
24:19
Structure of 2,3-Di-O-Methylglucose
26:47
Part A
28:11
Part B
33:46
Section 7: Lipids
Fatty Acids & Triacylglycerols

54m 55s

Intro
0:00
Fatty Acids
0:32
Lipids Overview
0:34
Introduction to Fatty Acid
3:18
Saturated Fatty Acid
6:13
Unsaturated or Polyunsaturated Fatty Acid
7:07
Saturated Fatty Acid Example
7:46
Unsaturated Fatty Acid Example
9:06
Notation Example: Chain Length, Degree of Unsaturation, & Double Bonds Location of Fatty Acid
11:56
Example 1: Draw the Structure
16:18
Example 2: Give the Shorthand for cis,cis-5,8-Hexadecadienoic Acid
20:12
Example 3
23:12
Solubility of Fatty Acids
25:45
Melting Points of Fatty Acids
29:40
Triacylglycerols
34:13
Definition of Triacylglycerols
34:14
Structure of Triacylglycerols
35:08
Example: Triacylglycerols
40:23
Recall Ester Formation
43:57
The Body's Primary Fuel-Reserves
47:22
Two Primary Advantages to Storing Energy as Triacylglycerols Instead of Glycogen: Number 1
49:24
Two Primary Advantages to Storing Energy as Triacylglycerols Instead of Glycogen: Number 2
51:54
Membrane Lipids

38m 51s

Intro
0:00
Membrane Lipids
0:26
Definition of Membrane Lipids
0:27
Five Major Classes of Membrane Lipids
2:38
Glycerophospholipids
5:04
Glycerophospholipids Overview
5:05
The X Group
8:05
Example: Phosphatidyl Ethanolamine
10:51
Example: Phosphatidyl Choline
13:34
Phosphatidyl Serine
15:16
Head Groups
16:50
Ether Linkages Instead of Ester Linkages
20:05
Galactolipids
23:39
Galactolipids Overview
23:40
Monogalactosyldiacylglycerol: MGDG
25:17
Digalactosyldiacylglycerol: DGDG
28:13
Structure Examples 1: Lipid Bilayer
31:35
Structure Examples 2: Cross Section of a Cell
34:56
Structure Examples 3: MGDG & DGDG
36:28
Membrane Lipids, Part 2

38m 20s

Intro
0:00
Sphingolipids
0:11
Sphingolipid Overview
0:12
Sphingosine Structure
1:42
Ceramide
3:56
Subclasses of Sphingolipids Overview
6:00
Subclasses of Sphingolipids: Sphingomyelins
7:53
Sphingomyelins
7:54
Subclasses of Sphingolipids: Glycosphingolipid
12:47
Glycosphingolipid Overview
12:48
Cerebrosides & Globosides Overview
14:33
Example: Cerebrosides
15:43
Example: Globosides
17:14
Subclasses of Sphingolipids: Gangliosides
19:07
Gangliosides
19:08
Medical Application: Tay-Sachs Disease
23:34
Sterols
30:45
Sterols: Basic Structure
30:46
Important Example: Cholesterol
32:01
Structures Example
34:13
The Biologically Active Lipids

48m 36s

Intro
0:00
The Biologically Active Lipids
0:44
Phosphatidyl Inositol Structure
0:45
Phosphatidyl Inositol Reaction
3:24
Image Example
12:49
Eicosanoids
14:12
Arachidonic Acid & Membrane Lipid Containing Arachidonic Acid
18:41
Three Classes of Eicosanoids
20:42
Overall Structures
21:38
Prostagladins
22:56
Thromboxane
27:19
Leukotrienes
30:19
More On The Biologically Active Lipids
33:34
Steroid Hormones
33:35
Fat Soluble Vitamins
38:25
Vitamin D₃
40:40
Vitamin A
43:17
Vitamin E
45:12
Vitamin K
47:17
Section 8: Energy & Biological Systems (Bioenergetics)
Thermodynamics, Free Energy & Equilibrium

45m 51s

Intro
0:00
Thermodynamics, Free Energy and Equilibrium
1:03
Reaction: Glucose + Pi → Glucose 6-Phosphate
1:50
Thermodynamics & Spontaneous Processes
3:31
In Going From Reactants → Product, a Reaction Wants to Release Heat
6:30
A Reaction Wants to Become More Disordered
9:10
∆H < 0
10:30
∆H > 0
10:57
∆S > 0
11:23
∆S <0
11:56
∆G = ∆H - T∆S at Constant Pressure
12:15
Gibbs Free Energy
15:00
∆G < 0
16:49
∆G > 0
17:07
Reference Frame For Thermodynamics Measurements
17:57
More On BioChemistry Standard
22:36
Spontaneity
25:36
Keq
31:45
Example: Glucose + Pi → Glucose 6-Phosphate
34:14
Example Problem 1
40:25
Question
40:26
Solution
41:12
More on Thermodynamics & Free Energy

37m 6s

Intro
0:00
More on Thermodynamics & Free Energy
0:16
Calculating ∆G Under Standard Conditions
0:17
Calculating ∆G Under Physiological Conditions
2:05
∆G < 0
5:39
∆G = 0
7:03
Reaction Moving Forward Spontaneously
8:00
∆G & The Maximum Theoretical Amount of Free Energy Available
10:36
Example Problem 1
13:11
Reactions That Have Species in Common
17:48
Example Problem 2: Part 1
20:10
Example Problem 2: Part 2- Enzyme Hexokinase & Coupling
25:08
Example Problem 2: Part 3
30:34
Recap
34:45
ATP & Other High-Energy Compounds

44m 32s

Intro
0:00
ATP & Other High-Energy Compounds
0:10
Endergonic Reaction Coupled With Exergonic Reaction
0:11
Major Theme In Metabolism
6:56
Why the ∆G°' for ATP Hydrolysis is Large & Negative
12:24
∆G°' for ATP Hydrolysis
12:25
Reason 1: Electrostatic Repulsion
14:24
Reason 2: Pi & Resonance Forms
15:33
Reason 3: Concentrations of ADP & Pi
17:32
ATP & Other High-Energy Compounds Cont'd
18:48
More On ∆G°' & Hydrolysis
18:49
Other Compounds That Have Large Negative ∆G°' of Hydrolysis: Phosphoenol Pyruvate (PEP)
25:14
Enzyme Pyruvate Kinase
30:36
Another High Energy Molecule: 1,3 Biphosphoglycerate
36:17
Another High Energy Molecule: Phophocreatine
39:41
Phosphoryl Group Transfers

30m 8s

Intro
0:00
Phosphoryl Group Transfer
0:27
Phosphoryl Group Transfer Overview
0:28
Example: Glutamate → Glutamine Part 1
7:11
Example: Glutamate → Glutamine Part 2
13:29
ATP Not Only Transfers Phosphoryl, But Also Pyrophosphoryl & Adenylyl Groups
17:03
Attack At The γ Phosphorous Transfers a Phosphoryl
19:02
Attack At The β Phosphorous Gives Pyrophosphoryl
22:44
Oxidation-Reduction Reactions

49m 46s

Intro
0:00
Oxidation-Reduction Reactions
1:32
Redox Reactions
1:33
Example 1: Mg + Al³⁺ → Mg²⁺ + Al
3:49
Reduction Potential Definition
10:47
Reduction Potential Example
13:38
Organic Example
22:23
Review: How To Find The Oxidation States For Carbon
24:15
Examples: Oxidation States For Carbon
27:45
Example 1: Oxidation States For Carbon
27:46
Example 2: Oxidation States For Carbon
28:36
Example 3: Oxidation States For Carbon
29:18
Example 4: Oxidation States For Carbon
29:44
Example 5: Oxidation States For Carbon
30:10
Example 6: Oxidation States For Carbon
30:40
Example 7: Oxidation States For Carbon
31:20
Example 8: Oxidation States For Carbon
32:10
Example 9: Oxidation States For Carbon
32:52
Oxidation-Reduction Reactions, cont'd
35:22
More On Reduction Potential
35:28
Lets' Start With ∆G = ∆G°' + RTlnQ
38:29
Example: Oxidation Reduction Reactions
41:42
More On Oxidation-Reduction Reactions

56m 34s

Intro
0:00
More On Oxidation-Reduction Reactions
0:10
Example 1: What If the Concentrations Are Not Standard?
0:11
Alternate Procedure That Uses The 1/2 Reactions Individually
8:57
Universal Electron Carriers in Aqueous Medium: NAD+ & NADH
15:12
The Others Are…
19:22
NAD+ & NADP Coenzymes
20:56
FMN & FAD
22:03
Nicotinamide Adenine Dinucleotide (Phosphate)
23:03
Reduction 1/2 Reactions
36:10
Ratio of NAD+ : NADH
36:52
Ratio of NADPH : NADP+
38:02
Specialized Roles of NAD+ & NADPH
38:48
Oxidoreductase Enzyme Overview
40:26
Examples of Oxidoreductase
43:32
The Flavin Nucleotides
46:46
Example Problems For Bioenergetics

42m 12s

Intro
0:00
Example 1: Calculate the ∆G°' For The Following Reaction
1:04
Example 1: Question
1:05
Example 1: Solution
2:20
Example 2: Calculate the Keq For the Following
4:20
Example 2: Question
4:21
Example 2: Solution
5:54
Example 3: Calculate the ∆G°' For The Hydrolysis of ATP At 25°C
8:52
Example 3: Question
8:53
Example 3: Solution
10:30
Example 3: Alternate Procedure
13:48
Example 4: Problems For Bioenergetics
16:46
Example 4: Questions
16:47
Example 4: Part A Solution
21:19
Example 4: Part B Solution
23:26
Example 4: Part C Solution
26:12
Example 5: Problems For Bioenergetics
29:27
Example 5: Questions
29:35
Example 5: Solution - Part 1
32:16
Example 5: Solution - Part 2
34:39
Section 9: Glycolysis and Gluconeogenesis
Overview of Glycolysis I

43m 32s

Intro
0:00
Overview of Glycolysis
0:48
Three Primary Paths For Glucose
1:04
Preparatory Phase of Glycolysis
4:40
Payoff Phase of Glycolysis
6:40
Glycolysis Reactions Diagram
7:58
Enzymes of Glycolysis
12:41
Glycolysis Reactions
16:02
Step 1
16:03
Step 2
18:03
Step 3
18:52
Step 4
20:08
Step 5
21:42
Step 6
22:44
Step 7
24:22
Step 8
25:11
Step 9
26:00
Step 10
26:51
Overview of Glycolysis Cont.
27:28
The Overall Reaction for Glycolysis
27:29
Recall The High-Energy Phosphorylated Compounds Discusses In The Bioenergetics Unit
33:10
What Happens To The Pyruvate That Is Formed?
37:58
Glycolysis II

1h 1m 47s

Intro
0:00
Glycolysis Step 1: The Phosphorylation of Glucose
0:27
Glycolysis Step 1: Reaction
0:28
Hexokinase
2:28
Glycolysis Step 1: Mechanism-Simple Nucleophilic Substitution
6:34
Glycolysis Step 2: Conversion of Glucose 6-Phosphate → Fructose 6-Phosphate
11:33
Glycolysis Step 2: Reaction
11:34
Glycolysis Step 2: Mechanism, Part 1
14:40
Glycolysis Step 2: Mechanism, Part 2
18:16
Glycolysis Step 2: Mechanism, Part 3
19:56
Glycolysis Step 2: Mechanism, Part 4 (Ring Closing & Dissociation)
21:54
Glycolysis Step 3: Conversion of Fructose 6-Phosphate to Fructose 1,6-Biphosphate
24:16
Glycolysis Step 3: Reaction
24:17
Glycolysis Step 3: Mechanism
26:40
Glycolysis Step 4: Cleavage of Fructose 1,6-Biphosphate
31:10
Glycolysis Step 4: Reaction
31:11
Glycolysis Step 4: Mechanism, Part 1 (Binding & Ring Opening)
35:26
Glycolysis Step 4: Mechanism, Part 2
37:40
Glycolysis Step 4: Mechanism, Part 3
39:30
Glycolysis Step 4: Mechanism, Part 4
44:00
Glycolysis Step 4: Mechanism, Part 5
46:34
Glycolysis Step 4: Mechanism, Part 6
49:00
Glycolysis Step 4: Mechanism, Part 7
50:12
Hydrolysis of The Imine
52:33
Glycolysis Step 5: Conversion of Dihydroxyaceton Phosphate to Glyceraldehyde 3-Phosphate
55:38
Glycolysis Step 5: Reaction
55:39
Breakdown and Numbering of Sugar
57:40
Glycolysis III

59m 17s

Intro
0:00
Glycolysis Step 5: Conversion of Dihydroxyaceton Phosphate to Glyceraldehyde 3-Phosphate
0:44
Glycolysis Step 5: Mechanism, Part 1
0:45
Glycolysis Step 5: Mechanism, Part 2
3:53
Glycolysis Step 6: Oxidation of Glyceraldehyde 3-Phosphate to 1,3-Biphosphoglycerate
5:14
Glycolysis Step 6: Reaction
5:15
Glycolysis Step 6: Mechanism, Part 1
8:52
Glycolysis Step 6: Mechanism, Part 2
12:58
Glycolysis Step 6: Mechanism, Part 3
14:26
Glycolysis Step 6: Mechanism, Part 4
16:23
Glycolysis Step 7: Phosphoryl Transfer From 1,3-Biphosphoglycerate to ADP to Form ATP
19:08
Glycolysis Step 7: Reaction
19:09
Substrate-Level Phosphorylation
23:18
Glycolysis Step 7: Mechanism (Nucleophilic Substitution)
26:57
Glycolysis Step 8: Conversion of 3-Phosphoglycerate to 2-Phosphoglycerate
28:44
Glycolysis Step 8: Reaction
28:45
Glycolysis Step 8: Mechanism, Part 1
30:08
Glycolysis Step 8: Mechanism, Part 2
32:24
Glycolysis Step 8: Mechanism, Part 3
34:02
Catalytic Cycle
35:42
Glycolysis Step 9: Dehydration of 2-Phosphoglycerate to Phosphoenol Pyruvate
37:20
Glycolysis Step 9: Reaction
37:21
Glycolysis Step 9: Mechanism, Part 1
40:12
Glycolysis Step 9: Mechanism, Part 2
42:01
Glycolysis Step 9: Mechanism, Part 3
43:58
Glycolysis Step 10: Transfer of a Phosphoryl Group From Phosphoenol Pyruvate To ADP To Form ATP
45:16
Glycolysis Step 10: Reaction
45:17
Substrate-Level Phosphorylation
48:32
Energy Coupling Reaction
51:24
Glycolysis Balance Sheet
54:15
Glycolysis Balance Sheet
54:16
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
Glycolysis IV

39m 47s

Intro
0:00
Feeder Pathways
0:42
Feeder Pathways Overview
0:43
Starch, Glycogen
2:25
Lactose
4:38
Galactose
4:58
Manose
5:22
Trehalose
5:45
Sucrose
5:56
Fructose
6:07
Fates of Pyruvate: Aerobic & Anaerobic Conditions
7:39
Aerobic Conditions & Pyruvate
7:40
Anaerobic Fates of Pyruvate
11:18
Fates of Pyruvate: Lactate Acid Fermentation
14:10
Lactate Acid Fermentation
14:11
Fates of Pyruvate: Ethanol Fermentation
19:01
Ethanol Fermentation Reaction
19:02
TPP: Thiamine Pyrophosphate (Functions and Structure)
23:10
Ethanol Fermentation Mechanism, Part 1
27:53
Ethanol Fermentation Mechanism, Part 2
29:06
Ethanol Fermentation Mechanism, Part 3
31:15
Ethanol Fermentation Mechanism, Part 4
32:44
Ethanol Fermentation Mechanism, Part 5
34:33
Ethanol Fermentation Mechanism, Part 6
35:48
Gluconeogenesis I

41m 34s

Intro
0:00
Gluconeogenesis, Part 1
1:02
Gluconeogenesis Overview
1:03
3 Glycolytic Reactions That Are Irreversible Under Physiological Conditions
2:29
Gluconeogenesis Reactions Overview
6:17
Reaction: Pyruvate to Oxaloacetate
11:07
Reaction: Oxaloacetate to Phosphoenolpyruvate (PEP)
13:29
First Pathway That Pyruvate Can Take to Become Phosphoenolpyruvate
15:24
Second Pathway That Pyruvate Can Take to Become Phosphoenolpyruvate
21:00
Transportation of Pyruvate From The Cytosol to The Mitochondria
24:15
Transportation Mechanism, Part 1
26:41
Transportation Mechanism, Part 2
30:43
Transportation Mechanism, Part 3
34:04
Transportation Mechanism, Part 4
38:14
Gluconeogenesis II

34m 18s

Intro
0:00
Oxaloacetate → Phosphoenolpyruvate (PEP)
0:35
Mitochondrial Membrane Does Not Have a Transporter for Oxaloactate
0:36
Reaction: Oxaloacetate to Phosphoenolpyruvate (PEP)
3:36
Mechanism: Oxaloacetate to Phosphoenolpyruvate (PEP)
4:48
Overall Reaction: Pyruvate to Phosphoenolpyruvate
7:01
Recall The Two Pathways That Pyruvate Can Take to Become Phosphoenolpyruvate
10:16
NADH in Gluconeogenesis
12:29
Second Pathway: Lactate → Pyruvate
18:22
Cytosolic PEP Carboxykinase, Mitochondrial PEP Carboxykinase, & Isozymes
18:23
2nd Bypass Reaction
23:04
3rd Bypass Reaction
24:01
Overall Process
25:17
Other Feeder Pathways For Gluconeogenesis
26:35
Carbon Intermediates of The Citric Acid Cycle
26:36
Amino Acids & The Gluconeogenic Pathway
29:45
Glycolysis & Gluconeogenesis Are Reciprocally Regulated
32:00
The Pentose Phosphate Pathway

42m 52s

Intro
0:00
The Pentose Phosphate Pathway Overview
0:17
The Major Fate of Glucose-6-Phosphate
0:18
The Pentose Phosphate Pathway (PPP) Overview
1:00
Oxidative Phase of The Pentose Phosphate Pathway
4:33
Oxidative Phase of The Pentose Phosphate Pathway: Reaction Overview
4:34
Ribose-5-Phosphate: Glutathione & Reductive Biosynthesis
9:02
Glucose-6-Phosphate to 6-Phosphogluconate
12:48
6-Phosphogluconate to Ribulose-5-Phosphate
15:39
Ribulose-5-Phosphate to Ribose-5-Phosphate
17:05
Non-Oxidative Phase of The Pentose Phosphate Pathway
19:55
Non-Oxidative Phase of The Pentose Phosphate Pathway: Overview
19:56
General Transketolase Reaction
29:03
Transaldolase Reaction
35:10
Final Transketolase Reaction
39:10
Section 10: The Citric Acid Cycle (Krebs Cycle)
Citric Acid Cycle I

36m 10s

Intro
0:00
Stages of Cellular Respiration
0:23
Stages of Cellular Respiration
0:24
From Pyruvate to Acetyl-CoA
6:56
From Pyruvate to Acetyl-CoA: Pyruvate Dehydrogenase Complex
6:57
Overall Reaction
8:42
Oxidative Decarboxylation
11:54
Pyruvate Dehydrogenase (PDH) & Enzymes
15:30
Pyruvate Dehydrogenase (PDH) Requires 5 Coenzymes
17:15
Molecule of CoEnzyme A
18:52
Thioesters
20:56
Lipoic Acid
22:31
Lipoate Is Attached To a Lysine Residue On E₂
24:42
Pyruvate Dehydrogenase Complex: Reactions
26:36
E1: Reaction 1 & 2
30:38
E2: Reaction 3
31:58
E3: Reaction 4 & 5
32:44
Substrate Channeling
34:17
Citric Acid Cycle II

49m 20s

Intro
0:00
Citric Acid Cycle Reactions Overview
0:26
Citric Acid Cycle Reactions Overview: Part 1
0:27
Citric Acid Cycle Reactions Overview: Part 2
7:03
Things to Note
10:58
Citric Acid Cycle Reactions & Mechanism
13:57
Reaction 1: Formation of Citrate
13:58
Reaction 1: Mechanism
19:01
Reaction 2: Citrate to Cis Aconistate to Isocitrate
28:50
Reaction 3: Isocitrate to α-Ketoglutarate
32:35
Reaction 3: Two Isocitrate Dehydrogenase Enzymes
36:24
Reaction 3: Mechanism
37:33
Reaction 4: Oxidation of α-Ketoglutarate to Succinyl-CoA
41:38
Reaction 4: Notes
46:34
Citric Acid Cycle III

44m 11s

Intro
0:00
Citric Acid Cycle Reactions & Mechanism
0:21
Reaction 5: Succinyl-CoA to Succinate
0:24
Reaction 5: Reaction Sequence
2:35
Reaction 6: Oxidation of Succinate to Fumarate
8:28
Reaction 7: Fumarate to Malate
10:17
Reaction 8: Oxidation of L-Malate to Oxaloacetate
14:15
More On The Citric Acid Cycle
17:17
Energy from Oxidation
17:18
How Can We Transfer This NADH Into the Mitochondria
27:10
Citric Cycle is Amphibolic - Works In Both Anabolic & Catabolic Pathways
32:06
Biosynthetic Processes
34:29
Anaplerotic Reactions Overview
37:26
Anaplerotic: Reaction 1
41:42
Section 11: Catabolism of Fatty Acids
Fatty Acid Catabolism I

48m 11s

Intro
0:00
Introduction to Fatty Acid Catabolism
0:21
Introduction to Fatty Acid Catabolism
0:22
Vertebrate Cells Obtain Fatty Acids for Catabolism From 3 Sources
2:16
Diet: Part 1
4:00
Diet: Part 2
5:35
Diet: Part 3
6:20
Diet: Part 4
6:47
Diet: Part 5
10:18
Diet: Part 6
10:54
Diet: Part 7
12:04
Diet: Part 8
12:26
Fats Stored in Adipocytes Overview
13:54
Fats Stored in Adipocytes (Fat Cells): Part 1
16:13
Fats Stored in Adipocytes (Fat Cells): Part 2
17:16
Fats Stored in Adipocytes (Fat Cells): Part 3
19:42
Fats Stored in Adipocytes (Fat Cells): Part 4
20:52
Fats Stored in Adipocytes (Fat Cells): Part 5
22:56
Mobilization of TAGs Stored in Fat Cells
24:35
Fatty Acid Oxidation
28:29
Fatty Acid Oxidation
28:48
3 Reactions of the Carnitine Shuttle
30:42
Carnitine Shuttle & The Mitochondrial Matrix
36:25
CAT I
43:58
Carnitine Shuttle is the Rate-Limiting Steps
46:24
Fatty Acid Catabolism II

45m 58s

Intro
0:00
Fatty Acid Catabolism
0:15
Fatty Acid Oxidation Takes Place in 3 Stages
0:16
β-Oxidation
2:05
β-Oxidation Overview
2:06
Reaction 1
4:20
Reaction 2
7:35
Reaction 3
8:52
Reaction 4
10:16
β-Oxidation Reactions Discussion
11:34
Notes On β-Oxidation
15:14
Double Bond After The First Reaction
15:15
Reaction 1 is Catalyzed by 3 Isozymes of Acyl-CoA Dehydrogenase
16:04
Reaction 2 & The Addition of H₂O
18:38
After Reaction 4
19:24
Production of ATP
20:04
β-Oxidation of Unsaturated Fatty Acid
21:25
β-Oxidation of Unsaturated Fatty Acid
22:36
β-Oxidation of Mono-Unsaturates
24:49
β-Oxidation of Mono-Unsaturates: Reaction 1
24:50
β-Oxidation of Mono-Unsaturates: Reaction 2
28:43
β-Oxidation of Mono-Unsaturates: Reaction 3
30:50
β-Oxidation of Mono-Unsaturates: Reaction 4
31:06
β-Oxidation of Polyunsaturates
32:29
β-Oxidation of Polyunsaturates: Part 1
32:30
β-Oxidation of Polyunsaturates: Part 2
37:08
β-Oxidation of Polyunsaturates: Part 3
40:25
Fatty Acid Catabolism III

33m 18s

Intro
0:00
Fatty Acid Catabolism
0:43
Oxidation of Fatty Acids With an Odd Number of Carbons
0:44
β-oxidation in the Mitochondrion & Two Other Pathways
9:08
ω-oxidation
10:37
α-oxidation
17:22
Ketone Bodies
19:08
Two Fates of Acetyl-CoA Formed by β-Oxidation Overview
19:09
Ketone Bodies: Acetone
20:42
Ketone Bodies: Acetoacetate
20:57
Ketone Bodies: D-β-hydroxybutyrate
21:25
Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 1
22:05
Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 2
26:59
Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 3
30:52
Section 12: Catabolism of Amino Acids and the Urea Cycle
Overview & The Aminotransferase Reaction

40m 59s

Intro
0:00
Overview of The Aminotransferase Reaction
0:25
Overview of The Aminotransferase Reaction
0:26
The Aminotransferase Reaction: Process 1
3:06
The Aminotransferase Reaction: Process 2
6:46
Alanine From Muscle Tissue
10:54
Bigger Picture of the Aminotransferase Reaction
14:52
Looking Closely at Process 1
19:04
Pyridoxal Phosphate (PLP)
24:32
Pyridoxamine Phosphate
25:29
Pyridoxine (B6)
26:38
The Function of PLP
27:12
Mechanism Examples
28:46
Reverse Reaction: Glutamate to α-Ketoglutarate
35:34
Glutamine & Alanine: The Urea Cycle I

39m 18s

Intro
0:00
Glutamine & Alanine: The Urea Cycle I
0:45
Excess Ammonia, Glutamate, and Glutamine
0:46
Glucose-Alanine Cycle
9:54
Introduction to the Urea Cycle
20:56
The Urea Cycle: Production of the Carbamoyl Phosphate
22:59
The Urea Cycle: Reaction & Mechanism Involving the Carbamoyl Phosphate Synthetase
33:36
Glutamine & Alanine: The Urea Cycle II

36m 21s

Intro
0:00
Glutamine & Alanine: The Urea Cycle II
0:14
The Urea Cycle Overview
0:34
Reaction 1: Ornithine → Citrulline
7:30
Reaction 2: Citrulline → Citrullyl-AMP
11:15
Reaction 2': Citrullyl-AMP → Argininosuccinate
15:25
Reaction 3: Argininosuccinate → Arginine
20:42
Reaction 4: Arginine → Orthinine
24:00
Links Between the Citric Acid Cycle & the Urea Cycle
27:47
Aspartate-argininosuccinate Shunt
32:36
Amino Acid Catabolism

47m 58s

Intro
0:00
Amino Acid Catabolism
0:10
Common Amino Acids and 6 Major Products
0:11
Ketogenic Amino Acid
1:52
Glucogenic Amino Acid
2:51
Amino Acid Catabolism Diagram
4:18
Cofactors That Play a Role in Amino Acid Catabolism
7:00
Biotin
8:42
Tetrahydrofolate
10:44
S-Adenosylmethionine (AdoMet)
12:46
Tetrahydrobiopterin
13:53
S-Adenosylmethionine & Tetrahydrobiopterin Molecules
14:41
Catabolism of Phenylalanine
18:30
Reaction 1: Phenylalanine to Tyrosine
18:31
Reaction 2: Tyrosine to p-Hydroxyphenylpyruvate
21:36
Reaction 3: p-Hydroxyphenylpyruvate to Homogentisate
23:50
Reaction 4: Homogentisate to Maleylacetoacetate
25:42
Reaction 5: Maleylacetoacetate to Fumarylacetoacetate
28:20
Reaction 6: Fumarylacetoacetate to Fumarate & Succinyl-CoA
29:51
Reaction 7: Fate of Fumarate & Succinyl-CoA
31:14
Phenylalanine Hydroxylase
33:33
The Phenylalanine Hydroxylase Reaction
33:34
Mixed-Function Oxidases
40:26
When Phenylalanine Hydoxylase is Defective: Phenylketonuria (PKU)
44:13
Section 13: Oxidative Phosphorylation and ATP Synthesis
Oxidative Phosphorylation I

41m 11s

Intro
0:00
Oxidative Phosphorylation
0:54
Oxidative Phosphorylation Overview
0:55
Mitochondrial Electron Transport Chain Diagram
7:15
Enzyme Complex I of the Electron Transport Chain
12:27
Enzyme Complex II of the Electron Transport Chain
14:02
Enzyme Complex III of the Electron Transport Chain
14:34
Enzyme Complex IV of the Electron Transport Chain
15:30
Complexes Diagram
16:25
Complex I
18:25
Complex I Overview
18:26
What is Ubiquinone or Coenzyme Q?
20:02
Coenzyme Q Transformation
22:37
Complex I Diagram
24:47
Fe-S Proteins
26:42
Transfer of H⁺
29:42
Complex II
31:06
Succinate Dehydrogenase
31:07
Complex II Diagram & Process
32:54
Other Substrates Pass Their e⁻ to Q: Glycerol 3-Phosphate
37:31
Other Substrates Pass Their e⁻ to Q: Fatty Acyl-CoA
39:02
Oxidative Phosphorylation II

36m 27s

Intro
0:00
Complex III
0:19
Complex III Overview
0:20
Complex III: Step 1
1:56
Complex III: Step 2
6:14
Complex IV
8:42
Complex IV: Cytochrome Oxidase
8:43
Oxidative Phosphorylation, cont'd
17:18
Oxidative Phosphorylation: Summary
17:19
Equation 1
19:13
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 Pump
28:48
Free Energy Change in Active Mitochondria
32:02
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Lecture Comments (11)

2 answers

Last reply by: Swati Sharma
Mon Apr 23, 2018 6:27 PM

Post by Swati Sharma on April 22, 2018

Dear Dr Rafi,

In class I haven't understood these three questions and would be grateful if you could explain these to me

1) Determine what reactions must be reversible and irreversible?
2)What reactions can potentially be the rate determining steps?
3)What reaction is the rate determining step?, the most important regulation point of glycolysis?

Regards
Swati

1 answer

Last reply by: Professor Hovasapian
Thu Jan 7, 2016 10:36 PM

Post by Rawan Shoair on January 1, 2016

I really am very thankful that a Prof. like you exists Prof. Raffi.

0 answers

Post by Peidong, He on December 11, 2014

You are awesome.

2 answers

Last reply by: Megan Ward
Fri May 2, 2014 7:52 AM

Post by Megan Ward on April 30, 2014

Hi Professor Hovasapian,
In the overall equation for glycolysis it is written that glucose+ 2ADP goes to products. I thought that it was ATP that was invested, not ADP?

1 answer

Last reply by: Professor Hovasapian
Thu Nov 21, 2013 1:01 AM

Post by Angela DiFabio on November 20, 2013

Hi Professor Hovasapian,

I have a question in regards to the amount of ATP produced if the cycle were to start with Sucroce? My teacher asked us this question and I wasn't sure exactly how to answer it. I do know that sucrose can be broken down into glucose and fructose - so does this mean that you would start with 1 molecule of glucose (net 2 ATP) and start with fructose additionally (net 3 ATP) for a total of 5 ATP?

Overview of Glycolysis I

Lecture Slides are screen-captured images of important points in the lecture. Students can download and print out these lecture slide images to do practice problems as well as take notes while watching the lecture.

  • Intro 0:00
  • Overview of Glycolysis 0:48
    • Three Primary Paths For Glucose
    • Preparatory Phase of Glycolysis
    • Payoff Phase of Glycolysis
    • Glycolysis Reactions Diagram
    • Enzymes of Glycolysis
  • Glycolysis Reactions 16:02
    • Step 1
    • Step 2
    • Step 3
    • Step 4
    • Step 5
    • Step 6
    • Step 7
    • Step 8
    • Step 9
    • Step 10
  • Overview of Glycolysis Cont. 27:28
    • The Overall Reaction for Glycolysis
    • Recall The High-Energy Phosphorylated Compounds Discusses In The Bioenergetics Unit
    • What Happens To The Pyruvate That Is Formed?

Transcription: Overview of Glycolysis I

Hello and welcome back to Educator.com, and welcome back to Biochemistry.0000

Today we are going to start off with something really, really exciting.0004

We have gone ahead and we are going to be starting a new unit; we are going to be starting glycolysis today, but more than that, we have actually done the first half of Biochemistry- the structure, the bioenergetics and things like that.0008

Now, we are going to start on the second half of biochemistry, which is metabolism; and this is really, really exciting.0019

This is the section that is actually going to be testing a lot of your memory.0028

There is going to be a lot of reactions going on; there is going to be lots of enzymes, lots of mechanisms, but all of it absolutely beautiful, I promise.0031

After all these years, I am still fascinated by how extraordinary this stuff is.0039

Anyway, we are going to get started with glycolysis, so let's jump right on in.0044

In this lesson, it is just going to be an overview; I am going to be talking about glycolysis globally, and then, in subsequent lessons, I am going to go through each individual step.0050

We are going to go through a detailed mechanism, structures- things like that.0059

OK, glucose is the primary sugar monomer that your body uses to create energy.0063

That is what is ultimately metabolized; that is what is broken down and run through the metabolic pathways, and all of the energy is extracted from that.0073

It is used to make the adenosine triphosphate; all of the carbons are oxidized to carbon dioxide.0084

And then, of course, it is oxidized to water, but it all begins with glucose.0091

Let's take a look at what glucose can do.0096

Glucose has 3 primary paths that it can follow.0101

When we say primary, most of it happens this way.0118

There are few other things that glucose can do, but most of glucose goes to these 3 things.0121

Let's go ahead and write glucose here.0129

We can take one path, and that is going to be the storage path.0133

No, that is fine; I will go ahead and...the body can take the glucose and create those polymers that we talked about when talked about carbohydrates, the starch and the glycogen.0138

It can use it for storage purposes; now, the other path that it can take is actually glycolysis, which we are going to talk about.0154

When it runs through glycolysis, the products are pyruvate + adenosine triphosphate.0165

OK, and the third path that it can take is something called the pentose phosphate pathway, and we are going to be discussing that after we discuss glycolysis.0174

And the final products of that particular pathway are the ribose 5-phosphate + NADH.0193

And you remember NADH is the reduced form of that particular coenzyme NAD+- oxidized form, reduced form.0209

OK, now, in glycolysis - glycolysis, if you like - a molecule of glucose is broken down into 2 molecules of pyruvate - and then absolutely, it is amazing, it still just amazes me, OK - in 10 enzyme catalyzed steps.0217

Of course, we know that every reaction in the body is catalyzed by an enzyme.0265

Now, glycolysis can be considered to have 2 phases.0280

Now, again, when we talk about these 2 phases, the preparatory phase, the payoff phase - or sometimes they call it the investment phase and the payoff phase - please understand that this is an artificial categorization based on how we want to look at things.0300

When things tend to get a little bit too complex, we like to break them down into smaller pieces.0314

Now, it is true; I mean, there is a preparatory phase and a payoff phase.0318

You will see what that means when we actually get into the details, but understand that you do not have to actually look at glycolysis that way if you do not want to.0322

This is just one, sort of, categorization of it.0328

I personally do not tend to look at it this way necessarily; I just look at it as 10 steps, 10 biochemical reactions, but I think it is great to, sort of, see it as preparatory or investment and then payoff.0333

Again, this is not set in stone; this is just a way of looking at something.0346

Do not feel like it is this, a glycolysis; there is this, and then there is that.0352

It is not; it is just our way of organizing the information.0357

OK, the first is called the preparatory phase or the investment phase.0360

OK, this is where glucose in 5 steps is converted to 2 molecules of glyceraldehyde 3-phosphate.0375

Now, the second phase is called the payoff phase, and this is where these 2 molecules, the glyceraldehyde 3-phosphate...I will just write it as 2 glyce 3P.0401

Again, in another 5 steps, you see the little bit of symmetry here that we have divided it into.0418

It is converted to 2 molecules of pyruvate- that is it, so preparatory phase, payoff phase.0426

A preparatory phase, investment phase, that is where ATP is used to actually invest a little bit more energy into the glucose molecule to actually prime it, to prepare it for the other reactions.0432

And the payoff phase comes because during that process, ATP is actually produced.0450

There is a net gain in adenosine triphosphate during glycolysis in addition to the pyruvate, so it is actually really, really great.0454

Now, let's go ahead and take a look at what is going on.0462

I am going to list the steps; I am going to list the actual enzymes that catalyze these steps.0469

And, of course, when we get into the details of the individual steps, we will talk a little bit more about the enzymatic activity.0472

OK, let's see what we have go here; this is your overview of glycolysis.0479

This is exactly what is happening; let me run through this really quickly.0484

You know what, let me go ahead and do it in blue just because I like blue.0489

We have glucose here; we start off with glucose, and some ATP is invested, and it converts it to glucose 6-phosphate.0497

The glucose 6-phosphate is then converted to fructose 6-phosphate.0507

Again, another ATP is used up; another ATP is invested in this to create fructose 1,6-biphosphate.0513

Now, this fructose 1,6-biphosphate is split in half; OK, we have 6, right?0521

Glucose is 6-carbon sugar, so it is split right down the middle- 3 carbons, 3 carbons.0526

And one of the things that it actually produces is directly glyceraldehyde 3-phosphate.0532

The other thing that it produces in this reaction is dihydroxyacetone phosphate; this is the DHAP.0538

Do not worry; we will be writing all of these things down.0546

And, of course, this is in your book; so I absolutely encourage you to look at the arrangement in your book.0549

Different books have different illustrations, and they are really fantastic.0555

This dihydroxyacetone phosphate is actually converted really quickly into glyceraldehyde 3-phosphate.0560

We end up with these 2 molecules; one molecule of glucose produces the 2 molecules of the glyceraldehyde 3-phosphate.0567

OK, now, each one of those goes through the same reaction.0575

This and this right here, the 2 columns- they are the same.0579

Glyceraldehyde 3-phosphate, inorganic phosphate, NAD+, is invested, and you end up oxidizing this, right?0582

Because, when this is oxidized, this NAD+ gets reduced.0593

NADH is produced, and it turns it into 1,3-biphosphoglycerate.0597

Well, now, ADP is put in; and ATP is produced in the step of converting the 1,3-biphosphoglycerate to the 3-phosphoglycerate.0602

3-phosphoglycerate is changed into 2-phosphoglycerate.0612

2-phosphoglycerate is converted to phosphoenolpyruvate; and the phosphoenolpyruvate, again, the ADP is brought in to create another molecule of ATP, and our final product is pyruvate.0617

Let's take a look at what is going on here.0630

We have 1, 2, 3, 4; 4 molecules of ATP are produced, but 2 are invested in the preparatory phase, so there is a net gain of 2 ATP molecules.0634

That is actually pretty, pretty great; I mean, basically this glycolysis pathway decides to use some of the extra energy to go ahead and create a little ATP in the process of breaking down the sugar, which it has to do, anyway.0647

That is what is magnificent about this; it is going to use up as much of the excess free energy that it can to do something that it can.0659

Now, most of the ATP in the body is not produced by this process; it is produced by oxidative phosphorylation, which we will talk about later, but it is kind of great that we are able to produce a little bit of ATP just to keep things going.0667

OK, let's number the steps here.0677

Let me see; should I do it on this side or that side?0683

I am going to do it here; this is step no. 1.0687

This is step no. 2; this is step 3.0691

This is step 4, and this is step 5.0695

When this breaks up, this, it produces a molecule of this and this.0699

We actually consider...I do not know.0705

If you want, we can consider this step 4; this step 4, this is probably best to do it this way.0709

And then, let's consider this step 5, the conversion of the dihydroxyacetone phosphate to the glyceraldehyde 3-phosphate.0713

OK, now, we have the other 5; we have 6.0721

This is step 7, step 8, step 9, and the final step, the conversion of the phosphoenolpyruvate to pyruvate.0726

OK, now, I am going to go ahead and write down the names of the enzymes just for the sake of seeing them.0735

One of the things that you want to do is you just want to see these things over and over again, the, sort of, passive learning process.0742

However - again, back to the actual learning - to learn these things, you actually have to write them down physically.0748

There is a deep connection between the actual physical active writing and the extent to which it actually stays in the brain.0753

My guess is you will have to actually memorize not just the molecules, but you will have to memorize the enzymes that catalyze these reactions.0762

OK, I am going to write no. 1 over here; the enzyme that catalyzes step 1 is hexokinase.0775

OK, no. 2, step 2 is phosphohexose isomerase or isomerase.0784

Again, you can do it anyway you want; step 3, we have phosphofructokinase-1 or PPK-1.0799

OK, the fourth enzyme is aldolase, and enzyme no. 5 is triosephosphate isomerase.0826

OK, now, let's come over here; you know what, I probably should have done that in black, but that is OK.0846

OK, now, enzyme no. 6, for this step right here, it is going to be glyceraldehyde 3-phosphate dehydrogenase.0851

Step 7 is catalyzed by phosphoglycerate kinase or kinase- it is up to you.0869

This is going to be no. 8, phosphoglycerate mutase.0886

I love these names; they are fantastic.0894

It is just they are really fantastic, and then, we have enolase.0896

And then, we have the pyruvate kinase- there you go.0901

This is the general scheme; 2 molecules of ATP are invested.0911

4 molecules of ATP are produced; there is a net gain of 2 molecules of ATP.0918

2 molecules of NADH are produced with their high-energy electrons; they can go on and do other things, reduce other things or enter the electron chain.0925

We have our enzymes; OK, now, let's go ahead and take a look at the structures of these molecules.0938

They are not just names; it is really, really important to because you are going to have to know what the structures are.0945

OK, let's start off with our...let's see; what should we do?0950

OK, alright; let's go ahead and start off with our glucose molecule here.0965

Let me see; I guess I will do it this way.0972

Alright, let's use this particular form: OH, OH, OH.0976

And then, of course, we have CH2; I think I am going to do the...that is OK.0985

I will go ahead and do the OH on this side; it is not a problem.0991

OK, this is our glucose molecule.0994

Should I do that in blue?1001

Yes, that is fine; OK, that is step 1.1003

Step 1, we are going to actually phosphorylate that thing right there, from glucose to glucose 6-phosphate.1007

We are going to have this.1015

It is just structures; it just takes a little while to write these things.1022

Also, you should know that I often do not write my hydrogens on carbons- sometimes I do, sometimes I do not.1029

Again, if there is a carbon that you see only has 2 bonds, the other 2 bonds are occupied by hydrogen- that is all that means.1034

OK, I will just go ahead and put a P here for the phosphoryl group.1043

OK, P, it is not PO4, the phosphoryl group.1050

This P is equivalent to PO32-; it is this molecule right here or this group.1057

It is this group that is attached to the...there is another oxygen here, but that oxygen comes from the alcohol that was attached to the carbon.1066

So, the phosphoryl group is actually PO32-; OK, not PO4.1074

It is not phosphate; it is a phosphoryl group.1077

OK, now, let's see.1080

Step 2, glucose 6-phosphate; now, we want to do fructose 6-phosphate.1085

Step 2 is going to look like this, boom, boom, boom, boom, here.1092

We will go ahead and put this here, CH2OH.1099

We have an OH here; I think it is going to be OH on top, OH on the bottom.1103

And then, of course, we have this C.1109

And then, we have this O, and you know what, I am going to go ahead and actually do it to the right, CO, P; how is that?1113

Fructose 6-phosphate, OK, let's see; should I go down, or should I go up?1125

How about if I go that way?1133

I will go that way, so step 3.1136

We are going to now, phosphorylate that one too.1140

So, we are going to have fructose 1,6-biphosphate; that is that, that, that.1145

We are going to have CH2, O, P.1150

We have OH; we have OH.1157

We have OH; there is still 6 carbons here, 1, 2, 3, 4, 5 and 6- there you go.1160

There is the CH2; there is the O, and there is the P.1168

This is fructose 1 - I am sorry - 1,6-biphosphate.1171

OK, now, we are going to actually split this up, and let me go ahead and just really quickly change.1178

The break is going to come right here.1185

OK, you are going to have this 3-carbon fragment and this 3-carbon fragment; and do not worry.1189

We will go through this again, but I just wanted you to see where the break actually takes place.1195

OK, and it does not take place while it is in its ring form; it takes place when it is in its extended form, its linear form.1200

That is the way it is attached in the enzyme; let me go back to blue.1207

Alright, from here, we go ahead and we create these 2 molecules.1212

Well, let me do it this way; let me go C, C, C.1222

There is that; there is this, glyceraldehyde-3-phosphate.1228

Let me just go ahead and put the P over here.1234

OK, this is our glyceraldehyde-3-phosphate, and it also produces the hydroxyacetone.1237

Let's go C, C, C.1243

Let me write it this way: CH2OH.1249

And then, let me just do H2; and well, I guess it does not really matter where we put the Hs and where we put the Os.1255

Let me just go ahead and put it over here.1266

This is in red; this is the dihydroxyacetone phosphate.1270

I am going to write it out: dihydroxyacetone phosphate.1278

And this is our glyceradehyde-3-phosphate, right?1290

Here is the aldehyde functional group; here is the phosphate.1299

Now, this thing right here, the dihydroxyacetone phosphate, that is the one that ends up getting converted.1303

OK, this is step 3; this is step 4, and we said step 5, and it gets converted to this right here.1309

Let me rewrite that again; we have C, C, C.1316

We have the aldehyde group; we have the hydroxy group, and we have the phosphate group, and that is fine.1321

I will go ahead and put those like that.1330

The hydroxyacetone phosphate is converted to another molecule of glyceraldehyde-3-phosphate.1334

This is glyceraldehyde-3-phosphate, here and here.1340

Step 4, when it breaks it up, it produces 1 molecule of the glyceraldehyde-3-phosphate directly.1348

The other one is converted into another molecule of glyceraldehyde-3-phosphate.1355

This is the preparatory phase, and these are the structures of the particular molecules.1360

OK, now, let's take a look at the rest of the structures.1364

Let me go to another page here; let me go back to blue.1370

We have glyceraldehyde-3-phosphate, C, C, C.1375

And again, you want to just keep drawing these things out over and over again.1382

Just look at your book and draw it; look at your book and draw it- that is all you have got to do.1386

It is just a process of getting used to; I know there is a lot of molecules to draw in biochemistry.1388

There is a lot of molecules to remember in biochemistry; some of them will only be passive recognition.1393

Some of them, you will have to be able to reproduce, but believe me, we all understand.1398

We have all been through it; we know how painful it can be.1402

OK, now, we have the O and the P; that is the glyceraldehyde-3-phosphate.1407

I will just write glyceraldehyde-3-phosphate over here.1415

Step 6 is going to convert it to 1,3-biphosphoglycerate.1420

We have C, C, C; and then we have O and a P.1425

Let me put a circle around the phosphate; we have our hydroxy group, and we have this over here, which stays, so 1,3-biphosphoglycerate.1431

Notice, this H was taken out; it was replaced by an O and a P.1440

OK, this is 1,3-biphosphoglycerate.1445

It is no longer glyceraldehyde; it is glycerate.1455

This is the carboxyl group; OK, step 7.1460

Now, this 1,3-biphosphoglycerate is going to be turned into 3-phosphoglycerate.1465

We are basically going to be getting rid of this phosphoryl group.1470

This is going to be C, C, C; and then we have this carboxy over here.1474

We have the OH over there, and we have our O and our P.1480

This is 3-phosphoglycerate, and I am hoping that you are going to confirm these structures.1484

Because again, as I am doing this, we all make mistakes.1491

I make a ton of them, so please confirm my structures; I might be missing a hydroxy.1497

I might be missing an oxygen; I might have an extra hydroxy- that happens.1501

OK, and then step 8, we want to change this into 2-phosphoglycerate; so we basically want to switch the P and the OH.1512

We will just write C, C, C.1522

I need a little bit more room here; no, that is OK.1529

OK, C, C, C, and then, we have this.1535

And then, of course, we have 2-phosphoglycerate; now, the phosphate group is there.1541

And now, the OH group is here, and I will go ahead and put that there.1545

This is going to be 2-phosphoglycerate.1552

OK, let's go ahead and do step 9; we are going to actually end up going to the next page.1562

Let's go ahead and we are going to be converting this to phosphoenolpyruvate.1568

We have got our 3 carbons still, C, C, C; but we have this beautiful double bond.1574

We have this, and we have O; and we have P.1584

Now, we have just the H2 there; this is the PEP.1589

This is the PEP, which is phosphoenolpyruvate.1595

And again, I do not know; I like separating my words.1603

Sometimes, they write them as 1; sometimes, they write them as 2.1606

It just depends how much of a strict what your teacher is.1608

That is the phosphoenolpyruvate, and, of course, our final conversion in glycolysis.1612

We are going to convert this phosphoenolpyruvate to pyruvate, which is C, C, C.1617

We have that, and we have this; and we have that.1625

This is our pyruvate.1631

There you go; those are the structures of the molecules involved in glycolysis, from 1 molecule of glucose going to 2 molecules of pyruvate.1638

OK, now, let's go ahead and talk about a little bit about the energetics.1648

Let me go back to black here; the overall reaction for glycolysis, when we take everything into account, everything that is happening, is as follows.1654

We have 1 molecule of glucose, 2 molecules of NAD+, 2 molecules of ADP plus 2 inorganic phosphates, produces 2 pyruvate plus 2 NADH plus 2 H+s plus 2 ATP plus 2 H2O.1671

That is the overall reaction; 1 glucose, 2 NAD+s, 2 ADPs, 2 PIs.1722

These are the molecules; these are the actual reactants, creates 2 pyruvates, 2 NADHs, 2 hydrogen ions, 2 molecules of ATP, and 2 molecules of water.1728

Now, we can resolve this, in other words, we can break it up into.1739

What this resolves into is the following; actually, let me go to the next page here.1743

OK, this resolves into the following.1750

We have 1 equation, which is actually the glucose plus the NA - oops, I have 2 of these - plus 2 of the NAD+, producing 2 pyruvate plus 2 NADH, plus 2H+1759

That is one of the reactions; now, the ΔG for this reaction is -146kJ/mol of glucose.1785

That is huge; it is a highly exergonic process.1796

Now, let's go ahead and take a look at this second part, the other part of this, the ADP.1800

2 ADP plus 2 PI goes to 2 ATP, the formation of adenosine triphosphate plus 2 H2O, in other words, the reverse of the hydrolysis of ATP.1807

We knew that the ATP hydrolysis is actually an exergonic process, but in this case, we are running it backwards.1821

We are taking ADP, and we are forming ATP; we are reversing hydrolysis.1826

We are doing a condensation here, and this one is going to be endergonic.1831

The ΔG for this, ΔG2 equals the +30.5 because we have reversed the reaction times 2 because now, it is 2 moles.1837

Oops, this is ADP.1849

I love it when you get all crazy into this, and all of a sudden, you are leaving letters off, which is very characteristic of me.1853

We have a +60 - I cannot even add - 61kJ.1860

So, this is an endergonic process, but notice, there is more than enough energy to account for this.1871

I mean, there is plenty of energy left; we can use part of this 146 to actually make the ATP in our process, and we still have more than enough free energy to carry this process forward.1876

ΔG, the net reaction is equal to the sum of the ΔGs: ΔG1 plus our ΔG2, which is equal to -146 plus our 61.1887

We have -85kJ/mol of glucose.1905

In glycolysis, even though some energy is invested into glucose by the 2 molecules of ATP, glucose by 2 ATPs, 4 ATPs are created by this coupling process, by coupling the highly exergonic glycolysis reactions to the endergonic ATP synthesis, to the endergonic ATP formation.1915

Now, recall back when we did bioenergetics.1992

OK, recall the high-energy phosphorylated compounds that we talked about in addition to ATP, high-energy phosphorylated compounds we discussed in the bioenergetics unit.2001

In addition to ATP, we talked about something; we talked about phosphoenolpyruvate.2040

We said that the free energy of hydrolysis of phosphoenolpyruvate - remember this equation, PEP + H2O, which goes to pyruvate + inorganic phosphate - the ΔG of this reaction was -61.9kJ/mol.2045

That is huge; that is a lot more than what is needed for ATP synthesis.2069

I mean, we know that ATP hydrolysis has -30.5kJ, so, its synthesis is +30.5kJ.2079

Well, we can couple that endergonic to a highly exergonic process, and this happens to be one of the reactions of glycolysis to actually create ATP in the process, rather than just wasting it.2089

We also had another one; we had the 1,3-biphosphoglycerate.2100

1,3- I will just write it as biphosphoglycerate.2106

That one also had a high negative free energy of hydrolysis, so 3-phosphoglycerate + inorganic phosphate.2112

This ΔG was -49.3; it is still very, very high.2124

This is kJ, not J; and notice, phosphoenolpyruvate and 1,3-biphosphoglycerate are intermediates in the glycolysis pathway.2130

So, we can use these reactions to actually make ATP.2140

These are 2 intermediates in the glycolytic pathway and have more than enough free energy to couple with ATP formation in the...2148

These are 2 intermediates in the glycolytic pathway and have more than enough free energy to couple with ATP formation in the process of glucose breakdown.2197

That is amazing; it is just truly amazing.2213

I love it; this is great.2219

I mean, the glucose has to be broken down, anyway; and this is just a highly exergonic process, especially with these two - the phosphoenolpyruvate and the 1,3biphosphoglycerate - that it is going to take that excess free energy and not just waste it.2221

It is going to use it to actually get back some of the ATP that it invested - in fact, create to, it used to - but it created for.2233

So, you actually have a net gain of adenosine triphosphate.2240

This is fantastic, using that excess energy that is going to be just wasted, anyway, use it to do something productive- absolutely fantastic.2244

OK, now, let's finish off this overview by discussing some of the fates of pyruvate.2253

What happens to the pyruvate that is formed in glycolysis; well, let's see.2257

No, let's go red; what the heck.2265

Actually, you know what, I think I am going to go blue.2272

The question is: what happens to the pyruvate that is formed?2280

Well, here is what happens; let's go ahead and write glucose, glucose, glycolysis.2297

We ended up forming 2 molecules of pyruvate.2306

Here is some of the things that happens.2313

OK, under aerobic conditions, in other words, when there is plenty of oxygen to go around, it is converted to 2 molecules of acetyl-CoA, which enters the citric acid cycle, which goes on to produce ultimately 3 electron transport chain, oxidate the phosphorylation, CO2, H2O and ATP.2317

This is the standard; this is what we are going to be running through.2343

It enters the citric acid cycle, and it goes through the oxidative phosphorylation cycle.2351

I will just go ahead and put electron transport chain.2360

You know what, no, I will just put oxidative phosphorylation, the end products being the CO2 plus the H2O- there you go.2365

That is under aerobic conditions, OK, pyruvate.2384

Under anaerobic conditions - in other words, no oxygen, not enough oxygen - it ends up producing the pyruvate.2390

It is converted to 2 molecules of lactate.2401

This is what you feel when your muscles start getting sore from overexertion.2406

The muscles are not getting enough oxygen to burn properly, to burn aerobically; so they have to turn to another process.2412

The by-product of that process is lactate, lactic acid.2421

That is what you feel when your muscles start to feel that sore, really painful feeling.2425

The pyruvate actually, it is fermentation.2434

The other fate is fermentation in heavily worked muscle.2441

OK, now, in general, I should say, fermentation is the general term for the breakdown or catabolism - I will write it over here, how is that - of organic molecules, nutrients, under low oxygen or no oxygen conditions.2453

It is a general term; when there is very little or no oxygen at all, the particular pathway, it is fermentation.2511

That is what is happening; it is fermenting.2519

And what you have in the third fate of pyruvate also under anaerobic or hypoxic - low oxygen as opposed to no oxygen - it will actually turn into ethanol.2523

This is how we get our drinking alcohol.2544

Ethanol + CO2- there you go.2548

Those are the fates of the pyruvate; the pyruvate will either go on to enter the citric acid cycle and go all the way in before they oxidized.2553

That is under aerobic conditions; under anaerobic conditions, it will produce lactate.2563

Under anaerobic and/or hypoxic conditions, under certain circumstances, it will end up forming ethanol and CO2.2568

That was our nice, broad overview of glycolysis.2579

In the next lesson and subsequent lessons, we are actually going to start looking at each individual step.2583

We are going to look at mechanisms, so we definitely, definitely want to make sure we understand glycolysis very, very well.2588

It is the model pathway for all the other metabolic pathways.2594

It is the one pathway that we elucidated first; it is the one that we understand the best.2598

Understanding what goes on here will pay multiple dividends in all of your future studies.2604

Take care; we will see you next time, bye-bye.2610

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