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Chapter 4 Cellular Metabolism
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About this Chapter Energy for synthesis and movement
Energy transformation Enzymes and how they speed reactions Metabolic pathways ATP its formation and uses in metabolism Synthesis of biologically important molecules
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Energy (E) Transfer Overview
Energy does work Kinetic energy Potential energy Energy conversion
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Energy (E) Transfer Overview
Figure 4-1: Energy transfer in the environment
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Chemosynthesis versus Photosynthesis
6CO2 + 6H2S → C6H12O6 + 6S Needs heat added such as from hydrothermal vents in the deep ocean Photosynthesis 2n CO2 + 2n H2O + photons → 2(CH2O)n + 2n O2 Occurs in Two Stages Stage 1: Light energy used to form ATP and NADPH Stage 2: Uses ATP and NADPH to reduce CO2
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Energy and Chemical Reactions
Figure 4-5: Energy transfer and storage in biological reactions
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Formation of ATP from Carbs, Proteins and Fat
Enzymes of metabolic pathways are able to capture the energy contained in carbohydrates, proteins and fatty acids in small portions and store it in form of internal high energy compounds such as ATP, drastically reducing the amount of energy lost as heat.
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Adenosine Triphosphate (ATP)
Source of immediately usable energy for the cell Adenine-containing RNA nucleotide with three phosphate groups
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Adenosine Triphosphate (ATP)
Figure 2.22
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How ATP Drives Cellular Work
Figure 2.23
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Protein Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds Figure 2.16
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Structural Levels of Proteins
Primary – amino acid sequence Secondary – alpha helices or beta pleated sheets
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Structural Levels of Proteins
Figure 2.17a-c
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Structural Levels of Proteins
Tertiary – superimposed folding of secondary structures Quaternary – polypeptide chains linked together in a specific manner
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Structural Levels of Proteins
Figure 2.17d, e
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Fibrous and Globular Proteins
Fibrous proteins Extended and strandlike proteins Examples: keratin, elastin, collagen, and certain contractile fibers Globular proteins Compact, spherical proteins with tertiary and quaternary structures Examples: antibodies, hormones, and enzymes
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Protein Synthesis Figure 4-34: Summary of transcription and translation
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Post – Translational protein modificaiton
Figure 4-35: Post-translational modification and the secretory pathway
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Post – Translational protein modificaiton
Folding, cleavage, additions: glyco- lipo- proteins
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Characteristics of Enzymes
Most are globular proteins that act as biological catalysts Holoenzymes consist of an apoenzyme (protein) and a cofactor (usually an ion) Enzymes are chemically specific Frequently named for the type of reaction they catalyze Enzyme names usually end in -ase Lower activation energy
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Characteristics of Enzymes
Figure 2.19
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Enzymes speed biochemical reactions
Figure 4-8: Two models of enzyme binding sites
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Mechanism of Enzyme Action
Enzyme binds with substrate Product is formed at a lower activation energy Product is released
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Enzymes speed biochemical reactions
Lower activation E Specific May require Cofactors or Coenzymes Modulators Acidity Temperature Competitive inhibitors Allosteric Concentrations
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Cofactors and Enzyme Activity
Cofactors are inorganic substrates. Some cofactors are required to produce a chemical reaction between the enzyme and the substrate, while others merely increase the rate of catalysis. Cofactors are sometimes attach to the enzyme, much like a prosthetic limb. Others are loosely bound to the enzyme.
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Coenzymes and Enzyme Activity
Unlike the inorganic cofactors, coenzymes are organic molecules. Certain enzymes need coenzymes to bind to the substrate and cause a reaction. Since the coenzymes are changed by the chemical reaction, these are considered to be secondary substrates of the reaction. Though enzymes are specific to the substrate, coenzymes are not specific to the enzymes they assist. Some chemical reactions within the cells of the body do require a cofactor or a coenzyme to work properly, while others do not. The body is unable to manufacture these products, so the way to get the vitamins necessary to produce cofactors and coenzymes is to eat a healthy, balanced diet full of all the vitamins necessary for bodily functions.
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Protein Denaturation Reversible unfolding of proteins due to drops in pH and/or increased temperature Figure 2.18a
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Protein Denaturation Irreversibly denatured proteins cannot refold and are formed by extreme pH or temperature changes Figure 2.18b
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Law of Mass Action Defined: Equlibrium Reversible
Figure 4-17: Law of mass action
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Types of Enzymatic Reactions
Oxidation–reduction Hydrolysis–dehydration Addition–subtraction exchange Ligation
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Figure 4-18b: A group of metabolic pathways resembles a road map
Cell Metabolism Pathways Intermediates Catabolic - energy Anabolic - synthesis Figure 4-18b: A group of metabolic pathways resembles a road map
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Control of Metabolic Pathways
Feedback inhibition Figure 4-19: Feedback inhibition
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ATP Production Glycolysis Pyruvate Anaerobic respiration
Lactate production 2 ATPs produced Figure 4-21: Overview of aerobic pathways for ATP Production
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Pyruvate Metabolism Aerobic respiration In mitochondria
Acetyl CoA and CO2 Citric Acid Cycle or Kreb’s Cycle or TCA Cycle Energy Produced from 1 Acetyl CoA 1 ATP 3 NADH 1 FADH2 Waste–2 CO2s
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Figure 4-23: Pyruvate metabolism
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Electron Transport High energy electrons Energy transfer
ATP synthesized from ADP H2O is a byproduct- In a typical individual this amounts to approximately 400 ml/day
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Electron Transport Figure 4-25: The electron transport system and ATP synthesis
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Biomolecules Catabolized to make ATP
Complex Carbohydrates Glycogen catabolism Liver storage Muscle storage Glucose produced Figure 4-26: Glycogen catabolism
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Protein Catabolism Deaminated Conversion Glucose Acetyl CoA
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Protein Catabolism Figure 4-27: Protein catabolism and deamination
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Lipid Catabolism Higher energy content Triglycerides to glycerol
Fatty acids Ketone bodies - liver
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Fat mass, adipose tissue and energy stores
Liver triglycerides = 450 kcal Muscle triglycerides = 3000 kcal Liver glycogen = 400 kcal Muscle glycogen = 2500 kcal Adipose tissue triglycerides = 120,000 kcal Data for a 70 kg lean subject.
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Synthetic (Anabolic) pathways
Glycogen synthesis Liver storage Glucose to glycogen Gluconeogenesis Amino acids Glycerol Lactate Figure 4-29: Gluconeogenesis
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Figure 4-30: Lipid synthesis
Lipogenesis Acetyl Co A Glycerol Fatty acids Triglycerides Figure 4-30: Lipid synthesis
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Figure 4-30: Lipid synthesis
Lipogenesis Figure 4-30: Lipid synthesis
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Summary Energy: chemical, transport, mechanical work
Reactions: reactants, activation energy, directions Enzymes: characteristics, speed & control pathways Metabolism: catabolic, anabolic ATP production: anaerobic, aerobic, glycolysis, citric acid cycle, & electron transport Synthesis of carbohydrates, lipids and proteins
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