AI Article Synopsis
- * The enzyme is quite adaptable to changes in the structure of glucose analogs, especially at the C-2 and C-3 positions, but is less forgiving with changes at C-1 and C-4.
- * The study also explores how certain inhibitors, like phosphoenolpyruvate and acetyl phosphate, affect hexokinase's function and the regeneration of ATP during these reactions.
Article Abstract
Yeast hexokinase (EC 2.7.1.1) catalyzes the phosphorylation of pyranose and furanose analogs of glucose at 0.01-125% of the rate of glucose. The enzyme is highly tolerant of structural changes at C-2 and C-3 of glucopyranose and less tolerant of changes at C-1 and C-4. Preparative phosphorylations were performed on compounds having 0.01-100% of the activity of glucose, using phosphoenolpyruvate and pyruvate kinase to regenerate ATP. The effects of inhibition of hexokinase by phosphoenolpyruvate and acetyl phosphate on cofactor regeneration are discussed.
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| http://dx.doi.org/10.1021/jo961715g | DOI Listing |
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