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Lecture24-2010 - Glycolysis 2 Lecture 24 Click to edit...

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Click to edit Master subtitle style Glycolysis 2 Lecture 24 Chapter 15, Sections 3 and 5
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Figure 15-1 Preparatory Stage Payoff Stage
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Page 497 Reaction 6: GAP dehydrogenase Dehydrogenases: involved in oxididation/reduction reactions. Couples favorable oxidation to unfavorable phosphorylation through covalent intermediate: thioester
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Figure 15-9 GAP dehydrogenase mechanism
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Page 499 Reaction 7: Phosphoglycerate kinase Substrate level phosphorylation
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PGK catalyzes a coupled reaction Favorable hydrolysis of 1,3-BPG coupled to unfavorable phosphorylation of ADP 1,3-BPG + H2O -----> 3PG + Pi Go’ = -49.3 kJ/mol ADP + Pi -----> ATP + H2O Go’ = +30.5 kJ/mol _________________________________________________ 1,3-BPG + ADP -----> 3PG + ATP Go’ = -18.8 kJ/mol
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GAP + Pi + NAD+ -----> 1,3-BPG + NADH + H+ Go’ = +6.7 kJ/mol 1,3-BPG + ADP -----> 3PG + ATP Go’ = -18.8 kJ/mol _________________________________________________ GAP + Pi + ADP + NAD+ -----> 3PG + ATP + NADH + H+ Go’ = -12.1 kJ/mol 1,3-BPG is a common intermediate between an unfavorable and favorable reaction
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Figure 15-12 Reaction 8: Phosphoglycerate mutase Mutase: subclass of isomerases, moves functional group from one position to another on substrate.
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Page 500 Where does phosphate come from? Priming reaction: 3PG kinase 3PG + ATP -------> 2,3-BPG + ADP Binds to PGM
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Page 500 Reaction 9: Enolase Reversible hydration/dehydration
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Page 501 Reaction 10: Pyruvate kinase Substrate level phosphorylation Largest free energy drop in Glycolysis (-61.9 kJ/mol) pulls entire pathway forward by mass action.
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