© 2014 Pearson Education, Inc. Chapter Opener 6

© 2014 Pearson Education, Inc. Chapter Opener 6

© 2014 Pearson Education, Inc. Figure 6-1 Converting potential energy to kinetic energy

© 2014 Pearson Education, Inc. Figure 6-1 Converting potential energy to kinetic energy

© 2014 Pearson Education, Inc. Figure 6-2 Energy conversions result in a loss of useful energy gas Combustion by engine 100 units chemical energy 80 units heat energy 20 units kinetic energy 

© 2014 Pearson Education, Inc. Figure 6-2 Energy conversions result in a loss of useful energy

© 2014 Pearson Education, Inc. Figure 6-3 An exergonic reaction reactants products energy

© 2014 Pearson Education, Inc. Figure 6-3 An exergonic reaction

© 2014 Pearson Education, Inc. Figure 6-4 An endergonic reaction reactants products energy

© 2014 Pearson Education, Inc. Figure 6-4 An endergonic reaction

© 2014 Pearson Education, Inc. Figure 6-5 Reactants and products of burning glucose 6 CO 2 energy (carbon dioxide) 6 H 2 O (water) 6 O 2 (oxygen) C 6 H 12 O 6 (glucose)  

© 2014 Pearson Education, Inc. Figure 6-5 Reactants and products of burning glucose

© 2014 Pearson Education, Inc. Figure 6-6 Photosynthesis 6 CO 2 energy (carbon dioxide) 6 H 2 O (water) 6 O 2 (oxygen) C 6 H 12 O 6 (glucose)  

© 2014 Pearson Education, Inc. Figure 6-6 Photosynthesis

© 2014 Pearson Education, Inc. Figure 6-7 Activation energy in an exergonic reaction Activation energy required to start the reaction products energy level of reactants energy content of molecules energy level of products progress of reaction An exergonic reaction Sparks ignite gas reactants high low

© 2014 Pearson Education, Inc. Figure 6-7 Activation energy in an exergonic reaction

© 2014 Pearson Education, Inc. Figure 6-7a An exergonic reaction Activation energy required to start the reaction products energy level of reactants energy content of molecules energy level of products progress of reaction An exergonic reaction reactants high low

© 2014 Pearson Education, Inc. Figure 6-7a An exergonic reaction

© 2014 Pearson Education, Inc. Figure 6-7b Sparks ignite gas Sparks ignite gas

© 2014 Pearson Education, Inc. Figure 6-7b Sparks ignite gas

© 2014 Pearson Education, Inc. Figure 6-8 The interconversion of ADP and ATP phosphate energy ATP ADP ATP energy phosphate ATP synthesis: Energy is stored in ATP ATP breakdown: Energy is released

© 2014 Pearson Education, Inc. Figure 6-8 The interconversion of ADP and ATP

© 2014 Pearson Education, Inc. Figure 6-8a ATP synthesis: Energy is stored in ATP phosphate energy ATP ADP ATP synthesis: Energy is stored in ATP

© 2014 Pearson Education, Inc. Figure 6-8a ATP synthesis: Energy is stored in ATP

© 2014 Pearson Education, Inc. Figure 6-8b ATP breakdown: Energy is released ADP ATP energy phosphate ATP breakdown: Energy is released

© 2014 Pearson Education, Inc. Figure 6-8b ATP breakdown: Energy is released

© 2014 Pearson Education, Inc. Figure 6-9 Coupled reactions within living cells high-energy reactants (glucose) ADP  P i high-energy products (protein) low-energy reactants (amino acids) low-energy products (CO 2, H 2 O) ATP exergonic (glucose breakdown) endergonic (protein synthesis)

© 2014 Pearson Education, Inc. Figure 6-9 Coupled reactions within living cells

© 2014 Pearson Education, Inc. Figure 6-10 Catalysts such as enzymes lower activation energy Activation energy without catalyst Activation energy with catalyst progress of reaction products reactants energy content of molecules high low

© 2014 Pearson Education, Inc. Figure 6-10 Catalysts such as enzymes lower activation energy

© 2014 Pearson Education, Inc. Figure 6-11 The cycle of enzyme–substrate interactions substrates active site of enzyme enzyme product Substrates enter the active site in a specific orientation The substrates and active site change shape, promoting a reaction between the substrates The substrates, bonded together, leave the enzyme; the enzyme is ready for a new set of substrates

© 2014 Pearson Education, Inc. Figure 6-11 The cycle of enzyme–substrate interactions

© 2014 Pearson Education, Inc. Slide 1 substrates enzyme active site of enzyme product Substrates enter the active site in a specific orientation The substrates and active site change shape, promoting a reaction between the substrates The substrates, bonded together, leave the enzyme; the enzyme is ready for a new set of substrates Figure 6-11 The cycle of enzyme substrate interactions

© 2014 Pearson Education, Inc. Slide 2 substrates enzyme active site of enzyme product Substrates enter the active site in a specific orientation Figure 6-11 The cycle of enzyme substrate interactions

© 2014 Pearson Education, Inc. Slide 3 substrates enzyme active site of enzyme product Substrates enter the active site in a specific orientation The substrates and active site change shape, promoting a reaction between the substrates Figure 6-11 The cycle of enzyme substrate interactions

© 2014 Pearson Education, Inc. Slide 4 substrates enzyme active site of enzyme product Substrates enter the active site in a specific orientation The substrates and active site change shape, promoting a reaction between the substrates The substrates, bonded together, leave the enzyme; the enzyme is ready for a new set of substrates Figure 6-11 The cycle of enzyme substrate interactions

© 2014 Pearson Education, Inc. Figure 6-12 Simplified metabolic pathways Initial reactant Intermediates End products PATHWAY 1 PATHWAY 2 enzyme 1 enzyme 2 enzyme 3 enzyme 4 enzyme 5 enzyme 6

© 2014 Pearson Education, Inc. Figure 6-12 Simplified metabolic pathways

© 2014 Pearson Education, Inc. Slide 1 Initial reactantIntermediatesEnd products enzyme 6enzyme 5 enzyme 4enzyme 3enzyme 2 PATHWAY 2 enzyme 1 PATHWAY 1 Figure 6-12 Simplified metabolic pathways

© 2014 Pearson Education, Inc. Slide 2 Initial reactant enzyme 1 PATHWAY 1 Figure 6-12 Simplified metabolic pathways

© 2014 Pearson Education, Inc. Slide 3 Initial reactantIntermediates enzyme 3enzyme 2enzyme 1 PATHWAY 1 Figure 6-12 Simplified metabolic pathways

© 2014 Pearson Education, Inc. Slide 4 Initial reactantIntermediatesEnd products enzyme 4enzyme 3enzyme 2enzyme 1 PATHWAY 1 Figure 6-12 Simplified metabolic pathways

© 2014 Pearson Education, Inc. Slide 5 Initial reactantIntermediatesEnd products enzyme 5 enzyme 4enzyme 3enzyme 2 PATHWAY 2 enzyme 1 PATHWAY 1 Figure 6-12 Simplified metabolic pathways

© 2014 Pearson Education, Inc. Slide 6 Initial reactantIntermediatesEnd products enzyme 6enzyme 5 enzyme 4enzyme 3enzyme 2 PATHWAY 2 enzyme 1 PATHWAY 1 Figure 6-12 Simplified metabolic pathways

© 2014 Pearson Education, Inc. Figure 6-13 Competitive and noncompetitive enzyme inhibition enzyme active site substrate noncompetitive inhibitor site noncompetitive inhibitor molecule The active site changes shape so the substrate no longer fits when a noncompetitive inhibitor molecule binds the enzyme A competitive inhibitor molecule occupies the active site and blocks entry of the substrate A substrate binding to an enzyme Competitive inhibition Noncompetitive inhibition

© 2014 Pearson Education, Inc. Figure 6-13 Competitive and noncompetitive enzyme inhibition

© 2014 Pearson Education, Inc. Slide 1 substrate active site enzyme noncompetitive inhibitor site A competitive inhibitor molecule occupies the active site and blocks entry of the substrate The active site changes shape so the substrate no longer fits when a noncompetitive inhibitor molecule binds the enzyme noncompetitive inhibitor molecule Figure 6-13 Competitive and noncompetitive enzyme inhibition A substrate binding to an enzyme Competitive inhibitionNoncompetitive inhibition

© 2014 Pearson Education, Inc. Slide 2 substrate active site enzyme noncompetitive inhibitor site Figure 6-13 Competitive and noncompetitive enzyme inhibition A substrate binding to an enzyme

© 2014 Pearson Education, Inc. Slide 3 substrate active site enzyme noncompetitive inhibitor site A competitive inhibitor molecule occupies the active site and blocks entry of the substrate Figure 6-13 Competitive and noncompetitive enzyme inhibition A substrate binding to an enzyme Competitive inhibition

© 2014 Pearson Education, Inc. Slide 4 substrate active site enzyme noncompetitive inhibitor site A substrate binding to an enzyme A competitive inhibitor molecule occupies the active site and blocks entry of the substrate Competitive inhibitionNoncompetitive inhibition The active site changes shape so the substrate no longer fits when a noncompetitive inhibitor molecule binds the enzyme noncompetitive inhibitor molecule Figure 6-13 Competitive and noncompetitive enzyme inhibition

© 2014 Pearson Education, Inc. Figure 6-13a A substrate binding to an enzyme enzyme active site substrate noncompetitive inhibitor site A substrate binding to an enzyme

© 2014 Pearson Education, Inc. Figure 6-13a A substrate binding to an enzyme

© 2014 Pearson Education, Inc. Figure 6-13b Competitive inhibition A competitive inhibitor molecule occupies the active site and blocks entry of the substrate Competitive inhibition

© 2014 Pearson Education, Inc. Figure 6-13b Competitive inhibition

© 2014 Pearson Education, Inc. Figure 6-13c Noncompetitive inhibition noncompetitive inhibitor molecule The active site changes shape so the substrate no longer fits when a noncompetitive inhibitor molecule binds the enzyme Noncompetitive inhibition

© 2014 Pearson Education, Inc. Figure 6-13c Noncompetitive inhibition

© 2014 Pearson Education, Inc. Figure 6-14 Allosteric regulation of an enzyme by feedback inhibition As levels of isoleucine rise, isoleucine binds to the regulatory site on enzyme 1, inhibiting it intermediates enzyme 1 enzyme 2 enzyme 3 enzyme 4 enzyme 5 enzyme 1 isoleucine (end product) threonine (initial reactant)

© 2014 Pearson Education, Inc. Figure 6-14 Allosteric regulation of an enzyme by feedback inhibition

© 2014 Pearson Education, Inc. Figure 6-15 Human enzymes function best within narrow ranges of pH and temperature For pepsin, maximum activity occurs at about pH 2 For most cellular enzymes, maximum activity occurs at about pH 7.4 For trypsin, maximum activity occurs at about pH 8 For most human enzymes, maximum activity occurs at about 98.6  F (37  C) rate of reaction rate of reaction fast slow Effect of pH on enzyme activity Effect of temperature on enzyme activity pH temperature (  C) (  F)

© 2014 Pearson Education, Inc. Figure 6-15 Human enzymes function best within narrow ranges of pH and temperature

© 2014 Pearson Education, Inc. Slide 1 fast slow rate of reaction pH For pepsin, maximum activity occurs at about pH 2 For trypsin, maximum activity occurs at about pH 8 For most cellular enzymes, maximum activity occurs at about pH 7.4 Effect of pH on enzyme activity fast slow rate of reaction For most human enzymes, maximum activity occurs at about 98.6°F (37°C) 32 0 temperature Effect of temperature on enzyme activity (°F) (°C) Figure 6-15 Human enzymes function best within narrow ranges of pH and temperature

© 2014 Pearson Education, Inc. Slide 2 fast slow rate of reaction pH For pepsin, maximum activity occurs at about pH 2 Effect of pH on enzyme activity fast slow rate of reaction 32 0 temperature Effect of temperature on enzyme activity (°F) (°C) Figure 6-15 Human enzymes function best within narrow ranges of pH and temperature

© 2014 Pearson Education, Inc. Slide 3 fast slow rate of reaction pH For pepsin, maximum activity occurs at about pH 2 For most cellular enzymes, maximum activity occurs at about pH 7.4 Effect of pH on enzyme activity fast slow rate of reaction 32 0 temperature Effect of temperature on enzyme activity (°F) (°C) Figure 6-15 Human enzymes function best within narrow ranges of pH and temperature

© 2014 Pearson Education, Inc. Slide 4 fast slow rate of reaction pH For pepsin, maximum activity occurs at about pH 2 For trypsin, maximum activity occurs at about pH 8 For most cellular enzymes, maximum activity occurs at about pH 7.4 Effect of pH on enzyme activity fast slow rate of reaction 32 0 temperature Effect of temperature on enzyme activity (°F) (°C) Figure 6-15 Human enzymes function best within narrow ranges of pH and temperature

© 2014 Pearson Education, Inc. Slide 5 fast slow rate of reaction pH For pepsin, maximum activity occurs at about pH 2 For trypsin, maximum activity occurs at about pH 8 For most cellular enzymes, maximum activity occurs at about pH 7.4 Effect of pH on enzyme activity fast slow rate of reaction For most human enzymes, maximum activity occurs at about 98.6°F (37°C) 32 0 temperature Effect of temperature on enzyme activity (°F) (°C) Figure 6-15 Human enzymes function best within narrow ranges of pH and temperature

© 2014 Pearson Education, Inc. Figure 6-15a Effect of pH on enzyme activity For pepsin, maximum activity occurs at about pH 2 For most cellular enzymes, maximum activity occurs at about pH 7.4 For trypsin, maximum activity occurs at about pH 8 rate of reaction fast slow Effect of pH on enzyme activity pH

© 2014 Pearson Education, Inc. Figure 6-15a Effect of pH on enzyme activity

© 2014 Pearson Education, Inc. Figure 6-15b Effect of temperature on enzyme activity For most human enzymes, maximum activity occurs at about 98.6  F (37  C) rate of reaction fast slow Effect of temperature on enzyme activity temperature 60 (  C) (  F)

© 2014 Pearson Education, Inc. Figure 6-15b Effect of temperature on enzyme activity

© 2014 Pearson Education, Inc. Figure E6-1 Risky behavior?

© 2014 Pearson Education, Inc. Figure E6-1 Risky behavior?

© 2014 Pearson Education, Inc. Unnumbered Figure Page 101

© 2014 Pearson Education, Inc. Unnumbered Figure Page 101