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Fundamentals of Biochemistry
Third Edition Donald Voet • Judith G. Voet • Charlotte W. Pratt Chapter 15 Glucose Catabolism Copyright © 2008 by John Wiley & Sons, Inc.
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Overview of Glycolysis
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Step 1 Not really that reversible
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Hexokinase
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Step 2
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Step 3
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Step 4
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Step 5
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Step 6
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Determination of the Mechanism
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Step 7
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Step 8
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Figure 15-12
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Step 9
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Step 10
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What did we accomplish? Overall, we took 1 glucose molecule and made: 2 pyruvates, 2 NADH, 2 ATP, and 2 H2O Net equation
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Fates of Pyruvate
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Lactate Dehydrogenase (LDH)
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Alcoholic Fermentation by Yeast
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Energy Efficiency ΔG°’ = -196 kJ/mol ΔG°’ = -235 kJ/mol
To make 2 ATP = ΔG°’ = 61 kJ/mol Therefore, lactate production is 61/196 = 31% efficient Therefore, ethanol production is 61/235 = 26% efficient Under biochemical concentrations, the reactions are actually >50% efficient
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Regulation of Glycolysis
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PFK is main regulatory enzyme
Activators: ADP; AMP; F2,6P Other substrate: F6P Substrate/inhibitor = ATP
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Other Mechanisms Is flux controlled only by ATP?
Seems like yes, but no Glycolytic flux varies by 100 fold ATP concentration varies only 10 fold ATP concentration is buffered by other enzymes such as creatine kinase and adenylate kinase However, [ATP] is 50X > [AMP] and 10x > [ADP] Therefore, a 10% change in [ATP] and result in 100% change of ADP and 400% change of AMP
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Substrate cycling A ↔ B If top equation were correct, then thermodynamics would be violated. One enzyme cannot be favorable in two directions Substrate cycling uses two different enzymes.
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Substrate cycling PFK FBPase
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Other Hexoses
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Pentose Phosphate Pathway
Stage 1 Stage 2 Stage 3
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Figure 15-34
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Figure 15-35
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