On the other hand, acyl phosphates, such as 1,3-bisphosphoglycerate, are more stable and undergo further enzyme-catalyzed transformation in cells. Predict the effects on the net reaction catalyzed by glyceraldehyde 3-phosphate dehydrogenase and other reactions of glycolysis if phosphate was replaced by arsenate.
The 1,3-bisphosphoglycerate intermediate would decompose nonenzymatically, so no NADH would be formed in the reaction.
There would be no net conversion of ADP to ATP from the conversion of glucose to pyruvate during glycolysis. Gluconeogenesis would be inhibited by arsenate because glyceraldehyde 3-phosphate dehydrogenase is also an enzyme in that pathway.
The 3-phosphoglycerate intermediate would decompose nonenzymatically, so no ATP would be formed in the phosphoglycerate kinase reaction.
By substituting for phosphate in this reaction, the arsenate-containing compounds would inhibit several downstream reactions.