Chapter 8: An Introduction to Metabolism. 1. Energy & Chemical Reactions 2. ATP 3. Enzymes & Metabolic Pathways
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1 Chapter 8: An Introduction to Metabolism 1. Energy & Chemical Reactions 2. ATP 3. Enzymes & Metabolic Pathways
2 1. Energy & Chemical Reactions
3 2 Basic Forms of Energy Kinetic Energy (KE) energy in motion or released energy: heat (molecular motion) electric current* (flow of charged particles) light energy* (radiation of photons) mechanical energy* (structural movement) chemical energy* (breaking covalent bonds, flow from high to low concentration) *forms of KE cells use to do things
4 Potential Energy (PE) stored energy (i.e., not yet released): A diver has more potential energy on the platform than in the water. Diving converts potential energy to kinetic energy. gravitational potential chemical bonds* chemical gradients*, charge gradients* Climbing up converts the kinetic energy of muscle movement to potential energy. A diver has less potential energy in the water than on the platform. *sources of PE cells rely on
5 Illustration of Kinetic & Potential Energy KE highest at b, lowest at a & c PE highest at a & c, lowest at b
6 Laws of Energy Transformation 1 st Law of Thermodynamics Energy is neither created Principle of Conservation of Energy: nor destroyed, but may be converted to other forms. Chemical energy Heat CO 2 + H 2 O (a) First law of thermodynamics (b) Second law of thermodynamics 2 nd Law of Thermodynamics Every energy transfer or every energy conversion results in a loss of usable energy as HEAT transformation increases the entropy of the universe.
7 Chemical Free Energy Gibb s Free Energy (G) = chemical PE DG = G products - G reactants Negative DG: loss of chemical PE (e.g., respiration) net release of KE (for work or to raise temperature) Positive DG: gain of chemical PE (e.g., photosynthesis) requires input of KE (e.g., sunlight) DG = 0: system is at equilibrium
8 Examples of Spontaneous Changes in Free Energy More free energy (higher G) Less stable Greater work capacity In a spontaneous change The free energy of the system decreases (DG 0) The system becomes more stable The released free energy can be harnessed to do work Less free energy (lower G) More stable Less work capacity (a) Gravitational motion (b) Diffusion (c) Chemical reaction in each case DG is negative and PE decreases
9 Free energy Free energy Exergonic Reactions Reactants net release of energy (DG is negative) Energy Products Amount of energy released ( G < 0) loss of PE Progress of the reaction (a) Exergonic reaction: energy released Endergonic Reactions Products net consumption of energy (DG is positive) Reactants Energy Amount of energy required ( G > 0) gain of PE Progress of the reaction (b) Endergonic reaction: energy required
10 Activation Energy (E A ) Whether endergonic or exergonic, all chemical reactions require some energy input for the reaction to proceed the A B activation C D energy (E A ) Transition state A B E A C D Reactants Progress of the reaction A B C D Products G < O all reactions require some sort of spark this is why sources of chemical PE are stable
11 Mechanical Model of Activation Energy The upright bottle falling over is analogous to an exergonic reaction, yet it still requires some energy input for the bottle to tip over.
12 3. ATP
13 ATP an Ideal Cellular Fuel useable amount of energy (DG -7.3 kcal/mole) stable, soluble in water (negatively charged) terminal phosphoanhydride bond easily broken
14 ATP Hydrolysis exergonic cleavage of terminal phospho-anhydride bond P P P Adenosine triphosphate (ATP) H 2 O DG -7.3 kcal/mole) P + P P i + Energy Inorganic phosphate Adenosine diphosphate (ADP)
15 The ATP Cycle ATP + H 2 O Energy from catabolism (exergonic, energy-releasing processes) ADP + P i Energy for cellular work (endergonic, energy-consuming processes) Exergonic processes (e.g., cellular respiration) provide energy for the endergonic synthesis of ATP, whereas ATP hydrolysis releases energy that can be used for other endergonic activities
16 Examples of ATP-powered Work Membrane protein P Solute P i Solute transported ATP (a) Transport work: ATP phosphorylates transport proteins ADP + Vesicle Cytoskeletal track P i ATP Motor protein Protein moved (b) Mechanical work: ATP binds noncovalently to motor proteins, then is hydrolyzed
17 Coupling of Biochemical Reactions Exergonic reactions fuel (provide energy for) endergonic reactions in cells (i.e, they are coupled ) exergonic endergonic exergonic breakdown of glucose fuels ATP production endergonic ATP hydrolysis fuels most cellular activities
18 Example of Coupling w/ ATP Hydrolysis (a) Glutamic acid conversion to glutamine Glu Glutamic acid NH 3 NH 2 Glu Ammonia Glutamine DG Glu = +3.4 kcal/mol (b) Conversion reaction coupled with ATP hydrolysis Glu Glutamic acid ATP 1 P 2 ADP Glu Phosphorylated intermediate NH 3 NH 2 Glu Glutamine ADP P i DG Glu = +3.4 kcal/mol (c) Free-energy change for coupled reaction Glu DG Glu = +3.4 kcal/mol + DG ATP = 7.3 kcal/mol NH 3 NH ATP 2 Glu DG ATP = 7.3 kcal/mol ADP P i Net DG = 3.9 kcal/mol
19 3. Enzymes & Metabolic Pathways
20 Enzymes are Biological Catalysts Biochemical reactions such as the one below will not occur spontaneously without a catalyst: Sucrase Sucrose (C 12 H 22 O 11 ) Glucose (C 6 H 12 O 6 ) Fructose (C 6 H 12 O 6 ) Enzymes are biological catalysts made of protein or RNA that determine when reactions occur. the production and regulation of enzymes give a cell complete control over all of the biochemical reactions that occur within the cell
21 Free energy Enzymes Lower Activation Energy Course of reaction without enzyme E A without enzyme E A with enzyme is lower Reactants Course of reaction with enzyme DG is unaffected by enzyme Progress of the reaction Products
22 Enzymes physically bind Substrates Active sites Substrate The fit of substrate into active site is highly specific and due to molecular complementarity Active site Substrate Enzyme Enzyme Enzyme-substrate complex Enzyme-substrate complex complementary in physical shape ( hand in glove ) complementary in chemical properties (attraction between opposite charges, hydrophobic regions)
23 The Catalytic Cycle of Enzymes 1 Enzyme available with empty active site Active site Substrate (sucrose) every enzyme has a unique substrate & thus catalyzes a specific reaction 2 Substrate binds to enzyme with induced fit Glucose Enzyme (sucrase) 4 Fructose Products are released 3 H 2 O Substrate is converted to products cells produce 1000s of different enzymes, all of which are proteins encoded by a particular gene
24 Rate of reaction Rate of reaction Factors effecting Enzyme Activity Optimal temperature for typical human enzyme Optimal temperature for enzyme of thermophilic (heat-tolerant) bacteria Temperature (ºC) (a) Optimal temperature for two enzymes Optimal temperature and ph for a given enzyme depend on the environment in which it normally functions Optimal ph for pepsin (stomach enzyme) Optimal ph for trypsin (intestinal enzyme) Deviation from the optimal conditions can result in denaturation and loss of enzyme activity ph (b) Optimal ph for two enzymes
25 Enzyme Regulation Substrate Active site Competitive inhibitor Enzyme (a) Normal binding (b) Competitive inhibition Noncompetitive inhibitor (c) Noncompetitive inhibition Enzymes can be regulated by inhibitors in two general ways: 1) Competition between inhibitor & substrate for active site 2) Remotely inducing the active site to change shape
26 Competitive Enzyme Inhibition Substrate Enzyme Competitive inhibitor Competitive inhibition involves binding of an inhibitor to the active site Reversible competitive inhibitor Substrate inhibitor must be reversible to be able to regulate in response to concentration Enzyme Increase in substrate concentration irreversible inhibitors essentially poison the enzyme
27 Allosteric Enzyme Regulation Allosteric regulation involves the binding of a substance to an enzyme outside the active site induces change in shape of active site Active site Enzyme Allosteric site Allosteric inhibition Distorted active site Substrate Substrate Distorted active site Allosteric inhibitor (non-competitive) Active site must be reversible Allosteric site Allosteric activation Allosteric activator
28 Cooperativity With many multimeric enzymes, the binding of substrate to one active site can stabilize the active conformation of other active sites, thus increasing the frequency with which they bind substrate. Substrate Inactive form Stabilized active form this is a type of allosteric regulation since active sites are regulated in a non-competitive manner (b) Cooperativity: another type of allosteric activation
29 Metabolic Pathways Most biological processes, whether anabolic (building) or catabolic (breaking down), require a series of chemical reactions (i.e., a pathway) Enzyme 1 Enzyme 2 Enzyme 3 A B C Reaction 1 Reaction 2 Reaction 3 Starting molecule D Product each step in a metabolic pathway is catalyzed by a specific enzyme a missing or inactive enzyme can prematurely shut down a metabolic pathway, leading to the accumulation of potentially dangerous intermediates
30 Initial substrate (threonine) Feedback Active site available Threonine in active site Inhibition Isoleucine used up by cell Feedback inhibition Active site of enzyme 1 no longer binds threonine; pathway is switched off. Intermediate A Enzyme 2 Intermediate B Enzyme 3 Enzyme 1 (threonine deaminase) The end-products of metabolic pathways can be important reversible enzyme inhibitors inhibit 1 st enzyme, turn pathway off Isoleucine binds to allosteric site Intermediate C Enzyme 4 Intermediate D Enzyme 5 low [inhibitor] = pathway ON high [inhibitor] = pathway OFF can be competitive or allosteric inhibition End product (isoleucine) important way of regulating end-product levels
31 Key Terms for Chapter 8 kinetic, potential energy, free energy endergonic, exergonic, coupling of reactions activation energy enzyme, catalyst substrate, active site, molecular complementarity competitive, noncompetitive, feedback inhibition allosteric, cooperative regulation reversible vs irreversible
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