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Consider the mechanism of cleavage catalyzed by the enzyme aldolase. What would be the products of...

Consider the mechanism of cleavage catalyzed by the enzyme aldolase. What would be the products of the reaction if aldolase used glucose-6-phosphate as the substrate, instead of fructose-1,6-bisphosphate (show the structures of glucose-6-phosphate and its products)? Based on your answer, suggest a possible rationale for why nature chose to include two extra steps prior to the aldolase step in glycolysis.

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Expert Solution

The step prior to the aldolase step is the isomerisation of glucose-6-phosphate to fructose-6-phosphate. The open-chain form of glucose has an aldehyde group at carbon 1, but the open-chain form of fructose has a keto group at carbon 2. Hence it can be said that the isomerization of glucose 6-phosphate to fructose 6-phosphate is a conversion of an aldose into a ketose. The reaction includes two extra steps prior to the aldolase step because both glucose 6-phosphate and fructose 6-phosphate are present primarily in the cyclic forms. The enzyme first opens the six-membered ring of glucose 6-phosphate, catalyze the isomerization, and then it promotes the formation of the five-membered ring of fructose 6-phosphate.

queen_honey_blossom answered 2 years ago
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