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Glycolysis: a mechanism you should know/ Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) 2. Carbonyl of GAP is attacked by cysteine, forming thiohemiacetal. 3. Thiohemiacetal is oxidized to a thioester by NAD*. 1. Substrate binds.

Glycolysis: a mechanism you should know/ Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) 2. Carbonyl of GAP is attacked by cysteine, forming thiohemiacetal. 3. Thiohemiacetal is oxidized to a thioester by NAD*. 1. Substrate binds.

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
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# Glycolysis: A Mechanism You Should Know ## Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) This diagram outlines the steps involved in the mechanism of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) during glycolysis. 1. **Substrate Binds** - NAD⁺ and a thiolate (HS) bind to the enzyme. The base (indicated as :B) is present. 2. **Formation of Thiohemiacetal** - The carbonyl of glyceraldehyde-3-phosphate (GAP) is attacked by the cysteine, forming thiohemiacetal. The reaction involves a covalent bond between the carbon (C) and sulfur (S). 3. **Oxidation to Thioester** - The thiohemiacetal is oxidized to a thioester by NAD⁺, resulting in the transfer of a hydride (H⁻) to NAD⁺, forming NADH. 4. **Thioester Intermediate** - The resulting structure is a thioester intermediate with NADH bound and a stabilized base (HB). 5. **Phosphate Attack and Product Formation** - An inorganic phosphate (P) binds and attacks the thioester. The product, 1,3-bisphosphoglycerate (1,3-bPG), is released. NADH is exchanged for NAD⁺, readying the enzyme for another cycle. ### Chemical Structures: - Each step includes detailed chemical structures with key atoms (C, H, O, S) and charge distribution. - The final product, 1,3-bisphosphoglycerate, features two phosphate groups connected to a glycerate backbone. This detailed mechanism highlights the enzymatic transformations critical in glycolysis, showcasing how GAPDH regulates energy production.
Transcribed Image Text:# Glycolysis: A Mechanism You Should Know ## Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) This diagram outlines the steps involved in the mechanism of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) during glycolysis. 1. **Substrate Binds** - NAD⁺ and a thiolate (HS) bind to the enzyme. The base (indicated as :B) is present. 2. **Formation of Thiohemiacetal** - The carbonyl of glyceraldehyde-3-phosphate (GAP) is attacked by the cysteine, forming thiohemiacetal. The reaction involves a covalent bond between the carbon (C) and sulfur (S). 3. **Oxidation to Thioester** - The thiohemiacetal is oxidized to a thioester by NAD⁺, resulting in the transfer of a hydride (H⁻) to NAD⁺, forming NADH. 4. **Thioester Intermediate** - The resulting structure is a thioester intermediate with NADH bound and a stabilized base (HB). 5. **Phosphate Attack and Product Formation** - An inorganic phosphate (P) binds and attacks the thioester. The product, 1,3-bisphosphoglycerate (1,3-bPG), is released. NADH is exchanged for NAD⁺, readying the enzyme for another cycle. ### Chemical Structures: - Each step includes detailed chemical structures with key atoms (C, H, O, S) and charge distribution. - The final product, 1,3-bisphosphoglycerate, features two phosphate groups connected to a glycerate backbone. This detailed mechanism highlights the enzymatic transformations critical in glycolysis, showcasing how GAPDH regulates energy production.
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