Question

The reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of deltaGo' for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. What is an explanation for why this reaction can be more favorable in vivo than it is under standard conditions (i.e. deltaG in the cell is more negative than deltaGo')?

Answer 1

In in vivo conditions the phosphate/Glucose1-phosphate ratio is more than 100 which supports the phosphorylation reacrion and hence this is better in comparison to that of standard condition.

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