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A pc8metabolism ppt


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A pc8metabolism ppt

  1. 1. Intro to Metabolism Campbell Chapter 8
  2. 2. <ul><li>Metabolism is the sum of an organism’s chemical reactions </li></ul><ul><li>Metabolism is an emergent property of life that arises from interactions between molecules within the cell </li></ul>
  3. 3. <ul><li>A metabolic pathway begins with a specific molecule and ends with a product </li></ul><ul><li>Each step is catalyzed by a specific enzyme </li></ul>BIOCHEMICAL PATHWAY VIDEO
  4. 4. ENZYMES THAT WORK TOGETHER IN A PATHWAY CAN BE Soluble with free floating intermediates Covalently bound in complex Attached to a membrane in sequence Biochemistry Lehninger Concentrated in specific location
  5. 5. <ul><li>CATABOLIC PATHWAY (CATABOLISM) Release of energy by the breakdown of complex molecules to simpler compounds EX: digestive enzymes break down food </li></ul><ul><li>ANABOLIC PATHWAY (ANABOLISM) consumes energy to build complicated molecules from simpler ones EX: linking amino acids to form proteins </li></ul>
  6. 6. Krebs Cycle connects the catabolic and anabolic pathways
  7. 7. Forms of Energy <ul><li>ENERGY = capacity to cause change </li></ul><ul><li>Energy exists in various forms (some of which can perform work) </li></ul><ul><li>Energy can be converted from one form to another </li></ul>
  8. 8. <ul><li>KINETIC ENERGY – energy associated with motion </li></ul><ul><ul><li>HEAT (thermal energy) is kinetic energy associated with random movement of atoms or molecules </li></ul></ul><ul><li>POTENTIAL ENERGY = energy that matter possesses because of its location or structure </li></ul><ul><ul><li>CHEMICAL energy is potential energy available for release in a chemical reaction </li></ul></ul>
  9. 9. On the platform, the diver has more potential energy. Diving converts potential energy to kinetic energy. Climbing up converts kinetic energy of muscle movement to potential energy. In the water, the diver has less potential energy.
  10. 10. <ul><li>THERMODYNAMICS = the study of energy transformations </li></ul><ul><li>CLOSED system (EX: liquid in a thermos) = isolated from its surroundings </li></ul><ul><li>OPEN system energy + matter can be transferred between the system and its surroundings </li></ul><ul><li>Organisms are open systems </li></ul>
  11. 11. The First Law of Thermodynamics <ul><li>= energy of the universe is constant </li></ul><ul><ul><li>Energy can be transferred and transformed </li></ul></ul><ul><ul><li>Energy cannot be created or destroyed </li></ul></ul><ul><li>The first law is also called the principle of CONSERVATION OF ENERGY </li></ul>
  12. 12. The Second Law of Thermodynamics <ul><li>During every energy transfer or transformation </li></ul><ul><li>entropy (disorder) of the universe INCREASES </li></ul><ul><li>some energy is unusable, often lost as heat </li></ul>
  13. 13. Chemical energy Heat CO 2 First law of thermodynamics Second law of thermodynamics H 2 O ORGANISMS are energy TRANSFORMERS! Spontaneous processes occur without energy input; they can happen quickly or slowly For a process to occur without energy input, it must increase the entropy of the universe
  14. 14. Free-Energy Change (  G) can help tell which reactions will happen <ul><li>∆ G = change in free energy ∆ H = change in total energy (enthalpy) or change ∆ S = entropy T = temperature </li></ul><ul><li> ∆ G = ∆ H - T ∆ S </li></ul><ul><li>Only processes with a negative ∆ G are spontaneous </li></ul><ul><li>Spontaneous processes can be harnessed to perform work </li></ul>
  15. 15. Exergonic and Endergonic Reactions in Metabolism <ul><li>EXERGONIC reactions (- ∆G) </li></ul><ul><li>Release energy </li></ul><ul><li>are spontaneous </li></ul><ul><li>ENDERGONIC reactions (+ ∆G) </li></ul><ul><li>Absorb energy from their surroundings </li></ul><ul><li>are non-spontaneous </li></ul>
  16. 16. Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions <ul><li>A cell does three main kinds of work: </li></ul><ul><ul><li>Mechanical </li></ul></ul><ul><ul><li>Transport </li></ul></ul><ul><ul><li>Chemical </li></ul></ul><ul><li>In the cell, the energy from the exergonic reaction of ATP hydrolysis can be used to drive an endergonic reaction </li></ul><ul><li>Overall, the coupled reactions are exergonic </li></ul>
  17. 17. Phosphate groups Ribose Adenine ATP (adenosine triphosphate) is the cell’s renewable and reusable energy shuttle ATP provides energy for cellular functions Energy to charge ATP comes from catabolic reactions
  18. 18. LE 8-9 Adenosine triphosphate (ATP) Energy P P P P P P i Adenosine diphosphate (ADP) Inorganic phosphate H 2 O + +
  19. 19. P i ADP Energy for cellular work provided by the loss of phosphate from ATP Energy from catabolism (used to charge up ADP into ATP ATP +
  20. 20. Endergonic reaction: D G is positive, reaction is not spontaneous Exergonic reaction: D G is negative, reaction is spontaneous  G = +3.4 kcal/mol  G = –7.3 kcal/mol  G = –3.9 kcal/mol NH 2 NH 3 Glu Glu Glutamic acid Coupled reactions: Overall D G is negative; Together, reactions are spontaneous Ammonia Glutamine ATP H 2 O ADP P i + + +
  21. 21. LE 8-11 NH 2 Glu P i P i P i P i Glu NH 3 P P P ATP ADP Motor protein Mechanical work: ATP phosphorylates motor proteins Protein moved Membrane protein Solute Transport work: ATP phosphorylates transport proteins Solute transported Chemical work: ATP phosphorylates key reactants Reactants: Glutamic acid and ammonia Product (glutamine) made + + +
  22. 22. Every chemical reaction between molecules involves bond breaking and bond forming ACTIVATION ENERGY = amount of energy required to get chemical reaction started Activation energy is often supplied in the form of heat from the surroundings IT’S LIKE PUSHING A SNOWBALL UP A HILL . . . Once you get it up there, it can roll down by itself Free energy animation
  23. 23. LE 8-14 Transition state C D A B E A Products C D A B  G < O Progress of the reaction Reactants C D A B Free energy The Activation Energy Barrier
  24. 24. <ul><li>CATALYST = a chemical agent that speeds up a reaction without being consumed by the reaction </li></ul><ul><li>ENZYMES = biological catalysts Most enzymes are PROTEINS Exception = ribozymes (RNA) Ch 17 & 26 </li></ul>
  25. 25. Course of reaction without enzyme E A without enzyme  G is unaffected by enzyme Progress of the reaction Free energy E A with enzyme is lower Course of reaction with enzyme Reactants Products ENZYMES work by LOWERING ACTIVATION ENERGY ;
  26. 26. ENZYMES LOWER ACTIVATION ENERGY BY <ul><ul><li>Orienting substrates correctly </li></ul></ul><ul><ul><li>Straining substrate bonds </li></ul></ul><ul><ul><li>Providing a favorable microenvironment </li></ul></ul><ul><li>Enzymes change ACTIVATION ENERGY but NOT energy of REACTANTS or PRODUCTS </li></ul>
  27. 27. ENZYMES <ul><li>Most are proteins </li></ul><ul><li>Lower activation energy </li></ul><ul><li>Specific </li></ul><ul><li>Shape determines function </li></ul><ul><li>Reusuable </li></ul><ul><li>Unchanged by reaction </li></ul>Image from:
  28. 28. <ul><li>The REACTANT that an enzyme acts on = SUBSTRATE </li></ul><ul><li>Enzyme + substrate = ENZYME-SUBSTRATE COMPLEX </li></ul><ul><li>Region on the enzyme where the substrate binds = ACTIVE SITE </li></ul><ul><li>Substrate held in active site by WEAK interactions (ie. hydrogen and ionic bonds ) </li></ul>
  29. 29. TWO MODELS PROPOSED <ul><li>LOCK & KEY Active site on enzyme fits substrate exactly </li></ul><ul><li>INDUCED FIT Binding of substrate causes change in active site so it fits substrate more closely </li></ul>
  30. 30. <ul><ul><li>General environmental factors, such as temperature, pH, salt concentration, etc. </li></ul></ul><ul><ul><li>Chemicals that specifically influence the enzyme </li></ul></ul> See a movie Choose narrated Enzyme Activity can be affected by:
  31. 31. <ul><li>TEMPERATURE & ENZYME ACTIVITY </li></ul><ul><li>Each enzyme has an optimal temperature at which it can function (Usually near body temp) </li></ul>
  32. 32. Increasing temperature increases the rate of an enzyme-catalyzed reaction up to a point. Above a certain temperature, activity begins to decline because the enzyme begins to denature .
  33. 33. pH and ENZYME ACTIVITY Each enzyme has an optimal pH at which it can function
  34. 34. <ul><li>CO FACTORS = non-protein enzyme helpers </li></ul><ul><li>EX: Zinc, iron, copper </li></ul><ul><li>CO ENZYMES = organic enzyme helpers </li></ul><ul><li>Ex: vitamins </li></ul>
  35. 35. SUBSTRATE CONCENTRATION & ENZYME ACTIVITY V MAX ← Adding substrate increases activity up to a point
  36. 36. REGULATION OF ENZYME PATHWAYS <ul><li>GENE REGULATION cell switches on or off the genes that code for specific enzymes </li></ul>
  37. 37. REGULATION OF ENZYME PATHWAYS <ul><li>FEEDBACK INHIBITION end product of a pathway interacts with and “turns off” an enzyme earlier in pathway </li></ul><ul><li>prevents a cell from wasting chemical resources by synthesizing more product than is needed </li></ul>FEEDBACK INHIBITION
  38. 38. <ul><li>NEGATIVE FEEDBACK </li></ul><ul><ul><li>An accumulation of an end product slows the process that produces that product </li></ul></ul>Example: sugar breakdown generates ATP; excess ATP inhibits an enzyme near the beginning of the pathway B A C D Enzyme 1 Enzyme 1 Enzyme 2 Enzyme 3 D D D D D D D D D D C B A Negative feedback
  39. 39. <ul><li>POSITIVE FEEDBACK (less common) </li></ul><ul><ul><li>The end product speeds up production </li></ul></ul>EXAMPLE: Chemicals released by platelets that accumulate at injury site, attract MORE platelets to the site. W W X Y Z Z Z Z Z Z Z Z Z Z Z Z Z Z Z Z Z Z Z Y X Enzyme 4 Enzyme 5 Enzyme 6 Enzyme 4 Enzyme 5 Enzyme 6 Positive feedback
  40. 40. REGULATION OF ENZYME ACTIVITY <ul><li>ALLOSTERIC REGULATION protein’s function at one site is affected by binding of a regulatory molecule at another site </li></ul><ul><li>Allosteric regulation can inhibit or stimulate an enzyme’s activity </li></ul> Allosteric enzyme inhibition
  41. 41. SOME ALLOSTERIC ENZYMES HAVE MULTIPLE SUBUNITS <ul><li>Each enzyme has active and inactive forms </li></ul><ul><li>The binding of an ACTIVATOR stabilizes the active form </li></ul><ul><li>The binding of an INHIBITOR stabilizes the inactive form </li></ul>
  42. 42. Substrate Binding of one substrate molecule to active site of one subunit locks all subunits in active conformation. Cooperativity another type of allosteric activation Stabilized active form Inactive form
  43. 43. COOPERATIVITY = form of allosteric regulation that can amplify enzyme activity Binding of one substrate to active site of one subunit locks all subunits in active conformation
  44. 44. COMPETITIVE inhibitor REVERSIBLE; Mimics substrate and competes with substrate for active site on enzyme ENZYMEANIMATION Enzyme Inhibitors
  45. 45. Enzyme Inhibitors <ul><li>NONCOMPETITIVE inhibitors bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective </li></ul>ENZYMEANIMATION