An Introduction to Metabolism
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1 Chapter 8 An Introduction to Metabolism oweroint Lectures for Biology, Seventh Edition Neil Campbell and Jane Reece Concept 8.1: An organism s metabolism transforms matter and energy, subject to the laws of thermodynamics Metabolism Is the totality of an organism s chemical reactions Arises from interactions between molecules Lectures by Chris Romero Organization of the Chemistry of Life into Metabolic athways A metabolic pathway has many steps That begin with a specific starting material and end with a product Each step is catalyzed by a specific enzyme Enzyme 1 Enzyme 2 Enzyme 3 A B C D Reaction 1 Reaction 2 Reaction 3 Starting roduct molecule Catabolic pathways Break down complex molecules into simpler compounds Release energy Anabolic pathways Build complicated molecules from simpler ones Consume energy Energy is the Capacity to Cause Change Kinetic energy Is the energy associated with motion otential energy Energy Circulates in Any Given System Energy can be converted From one form to another On the platform, a diver Diving converts potential has more potential energy. energy to kinetic energy. Is stored in the location of matter Includes chemical energy stored in molecular structure Figure 8.2 Climbing up converts kinetic energy of muscle movement to potential energy. In the water, a diver has less potential energy. 1
2 The First Law of Thermodynamics Thermodynamics Food rovides Energy to erform Work An example of energy conversion Is the study of energy transformations According to the first law of thermodynamics Energy can be transferred and transformed Chemical energy Energy cannot be created or destroyed Figure 8.3 (a) First law of thermodynamics: Energy can be transferred or transformed but Neither created nor destroyed. For example, the chemical (potential) energy in food will be converted to the kinetic energy of the cheetah s movement in (b). The Second Law of Thermodynamics According to the second law of thermodynamics Things fall apart Spontaneous changes that do not require outside energy increase the entropy, or disorder, of the universe Biological Order and Disorder Living systems do not violate the 2 nd law Increase the entropy of the universe Use energy to maintain order 50µm Heat co 2 + H 2O Figure 8.3 (b) Second law of thermodynamics: Every energy transfer or transformation increases the disorder (entropy) of the universe. For example, disorder is added to the cheetah s surroundings in the form of heat and the small molecules that are the by-products of metabolism. Figure 8.4 Concept 8.2: The free-energy change of a reaction tells us whether the reaction occurs spontaneously Free-Energy Change, ΔG A living system s free energy Is energy that can do work under cellular conditions The change in free energy, G during a biological process Is related directly to the enthalpy change ( H) and the change in entropy G = H T S 2
3 Free Energy, Stability, and Equilibrium Organisms live at the expense of free energy During a spontaneous change Free energy decreases and the stability of a system increases Equilibrium forward reaction = reverse reaction At maximum stability The system is at equilibrium More free energy (higher G) Less stable Greater work capacity In a spontaneously change The free energy of the system decreases ( G<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 Figure 8.5 (a) Gravitational motion. Objects (b) Diffusion. Molecules (c) Chemical reaction. In a move spontaneously from a in a drop of dye diffuse cell, a sugar molecule is higher altitude to a lower one. until they are randomly broken down into simpler dispersed. molecules. Exergonic and Endergonic Reactions in Metabolism An exergonic reaction all bets pay roceeds with a net release of free energy and is spontaneous Metabolism = endergonic + exergonic reactions An endergonic reaction you have made the house richer, but jackpot becomes larger for someone else Is one that absorbs free energy from its surroundings and is nonspontaneous Reactants roducts Free energy Energy roducts Amount of energy released ( G <0) Free energy Reactants Energy Amount of energy released ( G>0) rogress of the reaction rogress of the reaction Figure 8.6 (a) Exergonic reaction: energy released Figure 8.6 (b) Endergonic reaction: energy required Reactions can be described using Energy Diagrams A + B are the reactants C + D are the products This diagram follows the progress of an exergonic reaction Equilibrium and Metabolism Reactions in a closed system Eventually reach equilibrium G < 0 G = 0 Figure 8.7 A (a) A closed hydroelectric system. Water flowing downhill turns a turbine that drives a generator providing electricity to a light bulb, but only until the system reaches equilibrium. 3
4 Cells are open systems Cells in our body Experience a constant flow of materials in and out, preventing metabolic pathways from reaching equilibrium AT and Coupled Reactions Energy coupling Uses an exergonic reaction (favorable reaction) to provide energy to an endergonic (unfavorable) reaction (b) An open hydroelectric system. Flowing water keeps driving the generator because intake and outflow of water keep the system from reaching equlibrium. Figure 8.7 G < 0 Is a key feature in the way cells manage their energy resources to do this work AT The energy currency of the cell Concept 8.3: AT powers cellular work by coupling exergonic reactions to endergonic reactions The Structure and Hydrolysis of AT Energy is released from AT When the terminal phosphate bond is broken A cell does three main kinds of work Mechanical Transport Chemical i Adenosine triphosphate (AT) H 2 O + Energy Figure 8.9 Inorganic phosphate Adenosine diphosphate (AD) AT hydrolysis Can be coupled to other reactions Endergonic reaction: G is positive, reaction is not spontaneous Glu Glutamic acid AT + NH 3 + Ammonia H 2 O NH 2 Glu Glutamine Exergonic reaction: G is negative, reaction is spontaneous AD + G = +3.4 kcal/mol G = kcal/mol Coupled Reactions Which of the following reactions could be coupled to the reaction AT + H2O AD + i (-7.3 kcal/mol)? 1. A + i A (+10 kcal/mol) 2. B + i B (+8 kcal/mol) 3. C C + i (-4 kcal/mol) 4. D D + i (-10 kcal/mol) 5. E + i E (+5 kcal/mol) Figure 8.10 Coupled reactions: Overall G is negative; together, reactions are spontaneous G = 3.9 kcal/mol 4
5 How AT erforms Work AT drives endergonic reactions By phosphorylation, transferring a phosphate to other molecules The three types of cellular work Are powered by the hydrolysis of AT i The addition of a phosphate gives other molecules more free energy AT Motor protein rotein moved (a) Mechanical work: AT phosphorylates motor proteins Membrane protein AD + i i Solute Solute transported (b) Transport work: AT phosphorylates transport proteins NH 2 Glu + NH 3 + i Glu Figure 8.11 Reactants: Glutamic acid roduct (glutamine) and ammonia made (c) Chemical work: AT phosphorylates key reactants The Regeneration of AT Catabolic pathways Drive the regeneration of AT from AD and phosphate Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers A catalyst AT synthesis from AD + i requires energy AT hydrolysis to AD + i yields energy Is a chemical agent that speeds up a reaction without being consumed by the reaction AT An enzyme Is a catalytic protein (a protein catalyst) Energy from catabolism (exergonic, energy yielding processes) Energy for cellular work (endergonic, energyconsuming processes) Figure 8.12 AD + i Activation Energy The activation energy, E A Enzymes Lower the Activation Energy for a Rxn The effect of enzymes on reaction rate Is the initial amount of energy needed to start a chemical reaction Is often supplied in the form of heat from the surroundings in a system Free energy Course of reaction without enzyme Reactants Course of reaction with enzyme E A without enzyme E A with enzyme is lower G is unaffected by enzyme roducts Figure 8.15 rogress of the reaction 5
6 Substrate Specificity of Enzymes The substrate Is the reactant an enzyme acts on The enzyme s starting material The enzyme Binds to its substrate, forming an enzymesubstrate complex rotein shape determines what substrate will bind The active site Is the region on the enzyme where the substrate binds Substate Active site Enzyme Figure 8.16 (a) The substrate can change the shape of an enzyme Induced fit of a substrate Brings chemical groups of the active site into positions that enhance their ability to catalyze the chemical reaction The catalytic cycle of an enzyme 1 Substrates enter active site; enzyme changes shape so its active site embraces the substrates (induced fit). Substrates 6 Active site Is available for two new substrate Mole. Enzyme Enzyme-substrate complex 2 Substrates held in active site by weak interactions, such as hydrogen bonds and ionic bonds. 3 Active site (and R groups of its amino acids) can lower E A and speed up a reaction by acting as a template for substrate orientation, stressing the substrates and stabilizing the transition state, providing a favorable microenvironment, participating directly in the catalytic reaction. Figure 8.16 (b) Enzyme- substrate complex 5 roducts are Released. Figure 8.17 roducts 4 Substrates are Converted into roducts. How do Enzymes Function? Which of the following would be the same in an enzyme-catalyzed or -uncatalyzed reaction? a b c d e Enzyme Activity is Affected by Environmental Factors Each enzyme Has an optimal temperature in which it can function Rate of reaction Optimal temperature for typical human enzyme Optimal temperature for enzyme of thermophilic (heat-tolerant) bacteria Temperature (Cº) (a) Optimal temperature for two enzymes Figure
7 Environmental factors continued Has an optimal ph in which it can function Rate of reaction (b) Optimal ph for two enzymes Figure 8.18 Optimal ph for pepsin (stomach enzyme) Optimal ph for trypsin (intestinal enzyme) Environmental Factors and Enzyme Activity Which curve was generated using an enzyme taken from a bacterium that lives in hot springs at temperatures of 70ºC or higher? 1. curve 1 2. curve 2 3. curve 3 4. curve 4 5. curve 5 Enzyme Inhibitors Competitive inhibitors Bind to the active site of an enzyme, competing with the substrate A substrate can bind normally to the active site of an enzyme. Substrate Active site Noncompetitive inhibitors Bind to another part of an enzyme, changing the function (a) Normal binding A competitive inhibitor mimics the substrate, competing for the active site. Enzyme Competitive inhibitor A noncompetitive inhibitor binds to the enzyme away from the active site, altering the conformation of the enzyme so that its active site no longer functions. Noncompetitive inhibitor Figure 8.19 (c) Noncompetitive inhibition Figure 8.19 (b) Competitive inhibition Concept 8.5: Regulation of enzyme activity helps control metabolism A cell s metabolic pathways Feedback Inhibition In feedback inhibition The end product of a metabolic pathway shuts down the pathway Must be tightly regulated 7
8 Feedback Inhibition Feedback inhibition Active site available Initial substrate (threonine) Threonine in active site In the following branched metabolic pathway, a dotted arrow with a minus sign symbolizes inhibition of a metabolic step by an end product: Isoleucine used up by cell Feedback inhibition Isoleucine binds to allosteric site Figure 8.21 Enzyme 1 (threonine deaminase) Intermediate A Active site of Enzyme 2 enzyme 1 no longer binds threonine; Intermediate B pathway is switched off Enzyme 3 Intermediate C Enzyme 4 Intermediate D Enzyme 5 End product (isoleucine) Which reaction would prevail if both Q and S were present in the cell in high concentrations? 1. L M 2. M O 3. L N 4. O 5. R S 8
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