MadSci Network: Biochemistry |
Mauricio, The reason for the reversibility (or lack of it) in the kinase reactions you mention have to do with LeChatelier’s Principle. In the cell the concentration of ATP is typically much higher than that of ADP. The kinase reactions that are essentially irreversible in vivo are those that convert ATP into ADP. Phosphoglycerate kinase converts 1,3-diphosphoglycerate and ADP into 3-phosphoglycerate and ATP. Since the product ATP is present in high concentrations, this favors the reverse reaction. By contrast, the hexokinase reaction converts glucose and ATP into glucose-6-phosphate and ADP. Here, the high ATP concentration pushes the equilibrium so far to the right that in vivo the reverse reaction is essentially shut down. However the reverse reaction can be made to occur in vitro by supplying the enzyme with high concentrations of glucose-6-phosphate and ADP.
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