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Can the enzyme glucose isomerase, which converts glucose into fructose in the human body, perform the same reaction in a laboratory using a different enzyme?

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Final answer:

Phosphogluco-isomerase, an enzyme in glycolysis, converts glucose-6-phosphate into fructose-6-phosphate, and while similar reactions can occur in the lab with different enzymes or catalysts.

Step-by-step explanation:

The enzyme phosphogluco-isomerase, also known as glucose-6-phosphate isomerase, plays a crucial role in glycolysis by converting glucose-6-phosphate into fructose-6-phosphate. This reaction is facilitated by the principle that isomerases, such as phosphogluco-isomerase, catalyze the conversion of molecules into their isomers — compounds with the same chemical formula but different structures. In the laboratory, other enzymes or catalysts apart from glucose isomerase can be used to catalyze similar reactions, although conditions such as temperature and pH may vary, and the reaction may be slower compared to the enzymatic process in the human body.

In the glycolytic pathway, after the conversion to fructose-6-phosphate, further enzymatic actions take place leading to the eventual breakdown of glucose into two three-carbon molecules which are then utilized in subsequent energy-producing steps of glycolysis. In comparison, laboratory reactions may use different enzymes or even chemical catalysts like dilute acids to catalyze biochemical reactions, including the hydrolysis of other sugars like maltose or sucrose into their respective monosaccharides. However, these artificial processes generally require more time and higher temperatures to achieve the same result as the highly optimized enzyme-catalyzed reactions in the body.

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