1. Chapter 8 An Introduction To Metabolism

2. Metabolism u The totality of an organism’s chemical processes. u Concerned with managing the material and energy resources of the cell.

3. Catabolic Pathways u Pathways that break down complex molecules into smaller ones, releasing energy. u Example: Respiration

4. Anabolic Pathways u Pathways that consume energy, building complex molecules from smaller ones. u Example: Photosynthesis

5. Energy u Ability to do work. u The ability to rearrange a collection of matter. u Forms of energy: u Kinetic u Potential u Activation

7. Kinetic Energy u Energy of action or motion.

8. Potential Energy u Stored energy or the capacity to do work.

9. Activation Energy u Energy needed to convert potential energy into kinetic energy. Potential Energy Activation Energy

10. Energy Transformation u Governed by the Laws of Thermodynamics.

11. 1st Law of Thermodynamics u Energy can be transferred and transformed, but it cannot be created or destroyed. u Also known as the law of “Conservation of Energy”

12. 2nd Law of Thermodynamics u Each energy transfer or transformation increases the entropy (measure of disorder) of the universe.

13. Summary u The quantity of energy in the universe is constant, but its quality is not.

14. Question? u How does Life go against Entropy? u By using energy from the environment or external sources (e.g. food, light).

15. Free Energy u The portion of a system's energy that can perform work.

16. Chemical Reactions u Are the source of energy for living systems. u Are based on free energy changes.

17. Reaction Types u Exergonic: chemical reactions with a net release of free energy. u Endergonic: chemical reactions that absorb free energy from the surroundings.

18. Exergonic/Endergonic

19. Biological Examples u Exergonic - respiration u Endergonic - photosynthesis

20. Cell Energy u Couples an exergonic process to drive an endergonic one. u ATP is used to couple the reactions together.

22. ATP u Adenosine Triphosphate u Made of: - Adenine (nitrogenous base) - Ribose (pentose sugar) - 3 phosphate groups

24. Key to ATP u Is in the three phosphate groups. u Negative charges repel each other and makes the phosphates unstable.

25. ATP u Works by energizing other molecules by transferring phosphate groups.

26. ATP vs Food u ATP: u Renewable energy resource. u Unstable bonds u Food: u Long term energy storage u Stable bonds

27. ATP Cycles u Energy released from ATP drives anabolic reactions. u Energy from catabolic reactions “recharges” ATP.

28. ATP in Cells u A cell's ATP content is recycled every minute. u Humans use close to their body weight in ATP daily. u No ATP production equals quick death.

29. Enzymes u Biological catalysts made of protein. u Cause the rate of a chemical reaction to increase.

30. Enzymes u Lower the activation energy for a chemical reaction to take place.

32. Enzyme Terms u Substrate - the material an enzyme works on. u Enzyme names: Ex. Sucrase - ase name of an enzyme 1st part tells what the substrate is. (Sucrose)

33. Enzyme Name u Some older known enzymes don't fit this naming pattern. u Examples: pepsin, trypsin

34. Active Site u The area of an enzyme that binds to the substrate. u Structure is designed to fit the molecular shape of the substrate. u Therefore, each enzyme is substrate specific.

37. Models of How Enzymes Work 1. Lock and Key model 2. Induced Fit model

38. Lock and Key Model u Substrate (key) fits to the active site (lock) which provides a microenvironment for the specific reaction.

39. Induced Fit Model u Substrate “almost” fits into the active site, causing a strain on the chemical bonds, allowing the reaction.

40. Substrate Active Site

41. Enzymes u Usually specific to one substrate. u Each chemical reaction in a cell requires its own enzyme.

42. Factors that Affect Enzymes u Environment u Cofactors u Coenzymes u Inhibitors u Allosteric Sites

43. Environment u Factors that change protein structure will affect an enzyme. u Examples: u pH shifts u temperature u salt concentrations

44. u Cofactors: non-organic helpers to enzymes. Ex. Fe, Zn, Cu u Coenzymes: organic helpers to enzymes. Ex. vitamins

45. Enzyme Inhibitors u Competitive - mimic the substrate and bind to the active site. u Noncompetitive - bind to some other part of the enzyme and change active site structure.

47. Allosteric Regulation u The control of an enzyme complex by the binding of a regulatory molecule. u Regulatory molecule may stimulate or inhibit the enzyme complex.

48. Control of Metabolism u Is necessary if life is to function. u Controlled by switching enzyme activity "off" or "on” or separating the enzymes in time or space.

49. Types of Control u Feedback Inhibition u Structural Order

50. Feedback Inhibition u When a metabolic pathway is switched off by its end- product. u End-product usually inhibits an enzyme earlier in the pathway.

52. Structural Order u Separation of enzymes and metabolic pathways in time or space by the cell's organization. u Example: enzymes of respiration