1. Metabolism and Enzymes

2. Metabolism- the total of all chemical reactions done in an organism to store or release energy. (the number of molecules built vs. the amount of molecules broken down) ex. Digestion or building muscle. A metabolic pathway begins with a specific molecule and ends with a product and is carried out by enzymes. Metabolism

3. Catabolic pathways release energy by breaking down molecules into simpler compounds. Ex. Cellular respiration, the breakdown of glucose to release energy in humans. Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Catabolic Pathways

4. Anabolic pathways use energy to build molecules. The synthesis of protein from amino acids to be used in muscles is an example of anabolism. Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Anabolic Pathways

5. Thermodynamics Thermodynamics is the study of energy transformations Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

6. The First Law of Thermodynamics 1 st Law – energy cannot not by created or destroyed, just transformed. Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

7. The Second Law of Thermodynamics 2 nd Law - Every energy transfer increases the entropy (disorder) of the universe and makes things unstable. (energy will seek to get back into a stable form or equilibrium) Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

8. Free Energy free energy - energy available to do work ∆G = change in free energy If ∆G is negative energy was released (becomes more stable) If ∆G is positive energy was stored (becomes less stable) Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

9. Spontaneous Change Releasing free energy is known as a spontaneous change. The energy released in a spontaneous change can be harnessed to do work. Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

10. Fig. 8-5 (a) Gravitational motion (b) Diffusion(c) Chemical reaction More free energy (higher G) Less stable Greater work capacity In a spontaneous 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

12. An endergonic reaction absorbs free energy from its surroundings and is nonspontaneous. (Anabolic) Energy in Cells

13. An exergonic reaction proceeds with a net release of free energy and is spontaneous. (Catabolic) Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

14. Energy Coupling energy coupling - the use of an exergonic process to drive an endergonic one Most energy coupling in cells is done by ATP (the cells energy molecule). Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

15. ATP ATP (adenosine triphosphate) - ATP made of ribose (a sugar), adenine (a nitrogenous base), and three phosphate groups. Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

16. ATP powers cells by breaking off a phosphate group. This lowers free energy and releases energy. (exergonic) Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings ATP at Work

17. The released phosphate combines with a reactant (phosphorylation) to make it unstable. This endergonic reaction makes the recipient molecule unstable with extra stored energy and able to do work. Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

18. Fig. 8-11 (b) Mechanical work: ATP binds noncovalently to motor proteins, then is hydrolyzed Membrane protein P i ADP + P Solute Solute transported P i VesicleCytoskeletal track Motor protein Protein moved (a) Transport work: ATP phosphorylates transport proteins ATP

19. Fig. 8-12 P i ADP + ATP + H2OH2O Energy Coupling Dephosphorylation (exergonic) Phosphorylation (endergonic)

20. Enzymes catalyst - is a chemical agent that speeds up a reaction (can be reused) An enzyme is a catalytic protein Ex. Hydrolysis of sucrose by the enzyme sucrase

21. Activation Energy activation energy (E A ) -The initial energy needed to start a chemical reaction Activation energy can by supplied in the form of heat from the surroundings

22. Fig. 8-14 Progress of the reaction Products Reactants ∆G < O Transition state Free energy EAEA DC BA D D C C B B A A

23. Enzymes Lower the E A Enzymes catalyze reactions by lowering the E A barrier**** Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

24. Substrate Specificity of Enzymes substrate -reactant that an enzyme acts on enzyme- substrate complex – enzyme and substrate together active site – part of the enzyme the substrate binds to Induced fit – “lock and key” matching shape of enzyme and substrate Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

25. How E A is lowered The active site can lower an E A barrier by – Orienting substrates correctly – Straining substrate bonds – Providing favorable pH – Covalently bonding to the substrate Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

26. Fig. 8-17 Substrates Enzyme Products are released. Products Substrates are converted to products. Active site can lower E A and speed up a reaction. Substrates held in active site by weak interactions, such as hydrogen bonds and ionic bonds. Substrates enter active site; enzyme changes shape such that its active site enfolds the substrates (induced fit). Active site is available for two new substrate molecules. Enzyme-substrate complex 5 3 2 1 6 4

27. Enzyme Denature An enzyme’s activity can be affected by general environmental factors, such as temperature, pH, salinity, and solute concentration. Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

28. Cofactors Cofactors - are nonprotein enzyme helpers Coenzyme - An organic cofactor (ex. Vitamins) Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

29. Enzyme Inhibitors Competitive inhibitors bind to the active site of an enzyme, competing with the substrate Noncompetitive inhibitors bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective Examples of inhibitors include toxins, poisons, pesticides, and antibiotics Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings=

30. Allosteric Regulation of Enzymes Enzyme activity is controlled to regulate metabolism. Allosteric regulation - occurs when a regulatory molecule binds to a protein at one site and affects the protein’s function at another site. Inhibitors make enzymes inactive Activators make enzymes active Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

32. Cooperativity Cooperativity is a form of allosteric regulation where the presence of the substrate makes the enzyme active. Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

33. Feedback Inhibition In feedback inhibition, the end product of a metabolic pathway shuts down the pathway. Ex. thermostat. Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

34. You should now be able to: 1.Distinguish between the following pairs of terms: catabolic and anabolic pathways; exergonic and endergonic reactions 2.In your own words, explain the laws of thermodynamics. 3.Explain in general terms how cells obtain the energy to do cellular work Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

35. 4.Explain how ATP performs cellular work 5.Explain why an investment of activation energy is necessary to initiate a spontaneous reaction 6.Describe the mechanisms by which enzymes lower activation energy 7.Describe how allosteric regulators may inhibit or stimulate the activity of an enzyme Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings