Enzyme Hexokinase Reaction Phosphorylation Free Energy Change Standard

Enzyme: Hexokinase Reaction: Phosphorylation Free Energy Change: • Standard Conditions: -4. 0 kcal/mol • Physiological Conditions: -8. 0 kcal/mol irreversible Enzyme: Phosphoglucose isomerase Reaction: Aldose to Ketose Isomerisation Free Energy Change: • Standard Conditions: +0. 4 kcal/mol • Physiological Conditions: -0. 6 kcal/mol reversible Enzyme: Phosphofructokinase Reaction: Phosphorylation Free Energy Change: • Standard Conditions: -3. 4 kcal/mol • Physiological Conditions: -5. 3 kcal/mol irreversible

Enzyme: Aldolase Reaction: Aldol Cleavage Free Energy Change: • Standard Conditions: +5. 7 kcal/mol • Physiological Conditions: -0. 3 kcal/mol reversible Enzyme: Triose phosphate isomerase Reaction: Ketose to Aldose Isomerisation Free Energy Change • Standard Conditions: +1. 8 kcal/mol • Physiological Conditions: -+0. 6 kcal/mol reversible Enzyme: Glyceraldehyde 3 -phosphate dehydrogenase Reaction: Coupled Oxidation & Phosphorylation Free Energy Change • Standard Conditions: +1. 5 kcal/mol • Physiological Conditions: -0. 4 kcal/mol reversible

Enzyme: Phosphoglycerate kinase Reaction: Dephosphorylation Free Energy Change: • Standard Conditions: -4. 5 kcal/mol • Physiological Conditions: +0. 3 kcal/mol reversible Enzyme: Phosphoglyceromutase Reaction: Phosphate group shift Free Energy Change: • Standard Conditions: +1. 1 kcal/mol • Physiological Conditions: +0. 2 kcal/mol reversible

Enzyme: Enolase Reaction: Dehydration Free Energy Change: • Standard Conditions: +0. 4 kcal/mol • Physiological Conditions: -0. 8 kcal/mol reversible Enzyme: Pyruvate kinase Reaction: Dephosphorylation Free Energy Change: • Standard Conditions: -7. 5 kcal/mol • Physiological Conditions: -4. 0 kcal/mol irreversible Enzyme: Lactate dehydrogenase Reaction: Reduction Free Energy Change: • Standard Conditions: kcal/mol • Physiological Conditions: kcal/mol reversible

Enzyme: Citrate synthase Reaction: Condensation Acetyl Co. A condenses with oxaloacetate first, to form citryl Co. A. Then citryl Co. A is hydrolyzed to citrate and Co. A. Prosthetic group: No Enzyme: Aconitase Reaction: Dehydration Citrate is isomerized to isocitrate by this first dehydration and yields cis-aconitate as an intermediate. Prosthetic group: Fe-S Enzyme: Aconitase Reaction: Hydration of cis-aconitate gives the interchange of H atom and OH group from the step 2. Prosthetic group: Fe-S

Enzyme: Isocitrate dehydrogenase Reaction: Oxidative decarboxylation Dehydrogenation of isocitrate occurs and yields oxalosuccinate as an intermediate. Then CO 2 leaves to have alphaketoglutarate. This reaction gives NADH. Prosthetic group: No Enzyme: alpha-Ketoglutarate dehydrogenase complex Reaction: Oxidative decarboxylation This mechanism is almost as same as the reaction of the oxidative decarboxylation of pyruvate to acetyl Co. A by pyruvate dehydrogenase complex. This reaction gives one NADH. Prosthetic group: Lipoic acid, FAD, TPP Enzyme: Succinyl Co. A synthetase Reaction: Substrate-level phosphorylation The thioester bond of succinyl and Co. A is an energy rich bond. Thus only this step gives a high-energy phosphate compound, GTP from the couple reactions of the thioester bond cleavage and the phosphorylation of GDP. Prosthetic group: No

Enzyme: Succinate dehydrogenase Reaction: Oxidation The two hydrogens of succinate leave to an acceptor, FAD. Then this reaction yields fumarate and FADH 2. Prosthetic group: FAD & Fe-S Enzyme: Fumarase Reaction: Hydratation Fumarate is hydrated to give Malate. Prosthetic group: No Enzyme: Malate dehydrogenase Reaction: Oxidation Malate is dehydrogenated to form oxaloacetate. The hydrogen acceptor is NAD. So this reaction yields NADH. Prosthetic group: No