Let us imagine an enzyme that catalyzes the reaction below. The intermediate res

Question

Let us imagine an enzyme that catalyzes the reaction below. The intermediate resembles the transition state. Which of the to the molecules below would you expect to bind most tightly to the enzyme and why? Glycogen is treated with dimethylsulfate, which adds a methyl group to every free OH group. Next, the molecule is hydrolyzed to break all the glycoside bonds between glucose monomers, and these monomers are separated. Draw the structures of the methylated glucose monomers that result and circle the most abundant. (There are actually 4 types of monomers produced)

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I would suggest, but the question is not properly visible.

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