Ch 4: Energy and Cellular Metabolism
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1 Ch 4: Energy and Cellular Metabolism Energy as it relates to Biology Chemical reactions Enzymes and how they speed rxs Metabolism and metabolic pathways Catabolism (ATP production) Anabolism (Synthesis of biologically important molecules)
2 Energy in Biological Systems Review on your own!
3 Chemical Reactions 1. Transfer energy A + B Substrates / reactants C + D Products 2. or use energy to do work Bioenergetics: Study of energy flow through biol. systems Reaction rate = speed of reaction
4 Activation Energy Starts Reaction Fig 4-3 Reversible (most biol. rxs.) vs. irreversible reactions
5 Endergonic vs. Exergonic Reactions Which kind? Coupling endergonic and exergoinic rxs Direct coupling vs. indirect coupling
6 Enzymes are Proteins acting as Biological Catalysts 4 important characteristics of enzymes 1. chemical reaction rate by lowering activation energy 2. are not changed themselves 3. do not change nature of rx nor result 4. are specific Fig 4-8
7
8 Enzymes lower activation energy: All chemical reactions in body must be conducted at body temp.!! How do enzymes lower activation energy?
9 Enzymes bind to reactant molecules and bring them together in best position for rx.
10 Active Site: Small region of the complex 3D structure is active (or binding) site. Enzymes bind to substrate Old: Lock-and-key model / New: Induced-fit model Fig 2-16
11 Enzyme-substrate interaction: The old and the new model
12 Not in book Naming of Enzymes examples Kinase Phosphatase Peptidase Dehydrogenase mostly suffix -ase first part gives info on function
13 Isozymes = different models of same enzyme (differ in 1 or few aa) Examples: 1. Amylase Catalize same reaction under different conditions and in different tissues/organs 2. LDH importance in diagnostics Review Table 4-3
14 Enzyme Activity depends on 1. proteolytic activation (for some) 2. cofactors & coenzymes (for some) 3. temperature 4. ph 5. other molecules interacting with enzyme
15 1) Proteolytic Activation Also 1. Pepsinogen Pepsin 2. Trypsinogen Trypsin
16 2) Cofactors & Coenzymes structure: molecules (e.g.?) function: conformational change of active site structure: Organic molecules (vitamin derivatives, FADH 2...) function: act as receptors & carriers for atoms or functional groups that are removed from substrate
17 5) Molecules interacting with enzyme: Allosteric Modulators bind to enzyme away from active site changing shape of active site for better or for worse Allosteric Activator Fig 2-20 Allosteric Inhibitor
18 5) Molecules interacting with enzyme cont. Competitive inhibitors: reversible binding to active site block active site Fig 2-19 Also possible: irreversible binding via covalent bonds, e.g.: Penicillin Cyanide
19 Reversible Reactions follow the Law of Mass Action Fig 4-9
20 Three Major Types of Enzymatic Reactions: 1. Oxydation - Reduction reactions (transfer of?) 2. Hydrolysis - Dehydration reactions (breakdown & synthesis of?) 3. Addition-Subtraction-Exchange reactions
21
22 ?
23 Metabolism Catabolism Anabolism
24 Metabolism definition: Metabolic pathways = network of linked reactions Cells regulate metabolic pathways via 1. Control of enzyme concentration 2. Modulator production (allosteric modulators, feedback inhibition, Fig 4-11) 3. Different enzymes for reversible rxs, Fig 4-12) 4. Compartmentation of enzymes 5. ATP / ADP ratio
25 Metabolic pathways: Network of interconnected chemical reactions Linear pathway Intermediates Circular pathway Branched pathway
26 Special case: = end product inhibition Fig 4-11
27
28 Catabolic Pathways: ATP-Production Amount of ATP produced reflects on usefulness of metabolic pathways: Aerobic pathways Anaerobic pathways Different biomolecules enter pathway at different points
29 ATP = Energy Carrier of Cell (not very useful for energy storage) ATP Cycle ATP : ADP ratio determines status of ATP synthesis reactions
30 Glycolysis From 1 glucose to 2 pyruvate molecules Main catabolic pathway of cytoplasm Does not require O 2 part of and catabolism Starts with phosphorylation ( Before doubling your money you first have to invest! ) Fig 4-13
31 Pyruvate has 2 Possible Fates Anaerobic catabolism: Pyruvate lactate Aerobic catabolism: Pyruvate Citric Acid Cycle
32 Citric Acid Cycle Other names? Takes place in? Energy Produced: 1 ATP 3 NADH 1 FADH 2 Waste 2 CO 2 Fig. 4-16
33 Energy Yield of Krebs Cycle NADH Compare to Fig NADH NADH FADH 2
34 Final step: Electron Transport System Chemiosmotic theory / oxydative phosphorylation Transfers energy from NADH and FADH 2 to ATP (via e - donation and H + transport) Mechanism: Energy released by movement of e - trough transport system is stored temporarily in H + gradient NADH produces a maximum of 2.5 ATP FADH 2 produces a maximum of 1.5 ATP 1 ATP formed per 3H + shuttled through ATP Synthase Fig 4-17
35 Cellular Respiration Maximum potential yield for aerobic glucose metabolism: ATP synthesized from ADP H 2 O is a byproduct
36 Synthetic Pathways Anabolic rxs synthesize large biomolecules Unit molecules nutrients & energy required Macromolecules Polysaccharides Lipids DNA Protein
37 Glycogen Synthesis Made from glucose Stored in all cells but especially in Liver (keeps 4h glycogen reserve for between meals) Skeletal Muscle muscle contraction Gluconeogenesis Glycolysis in reverse From glycerol, aa and lactate All cells can make G-6-P, only liver and Kidney can make glucose
38 Protein Synthesis Proteins are the key to cell function necessary for all cell functions Protein synthesis is under nuclear direction DNA specifies Proteins?? DNA mrna Protein
39 How can only 4 bases in DNA encode > 20 different aa in protein? 1 letter word: 1 base = 1 aa how many possibilities? 2 letter word: 2 bases = 1 aa how many possibilities? 3 letter word: 3 bases = 1 aa how many possibilities? 3 letter words = base triplets or codons
40 Redundancy of Genetic Code 1 start codon (AUG = Met) 3 stop codons 60 other codons for 19 aa
41 Transcription DNA is transcribed into complementary mrna by RNA Polymerase + nucleotides + Mg 2+ ( =?) +? Gene = elementary unit of inheritance Compare to Fig and review Fig 4-26
42 Translation mrna is translated into string of aa (= polypeptide) 2 important components?? mrna + ribosomes + trna meet in cytoplasm Anticodon pairs with mrna codon aa determined Amino acids are linked via bond. Fig 4-27
43 Post Translational protein modifications: Folding, cleavage, additions glyco-, lipo- proteins Protein Sorting Due to signal/targeting sequence No targeting sequence protein stays in cytoplasm Targeting sequence protein destined for translocation into organelles or for export from cell
44 For export proteins : Signal sequence leads growing polypeptide chain across ER membrane into ER lumen Modifications in ER Transition vesicles to Compare to Fig 4-28 Golgi apparatus for further modifications Transport vesicles to cell membrane
45 DNA Replication Semiconservative DNA polymerase
46 Running problem: Tay-Sachs Disease
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