An enzymatic cleavage and phosphoryl transfer reaction involving monothiolphosphate

Abstract

Thiolphosphates have been suggested as intermediates in various activation processes, but conclusive evidence for their participation in these reactions has not been obtained. Recently, however, cysteamine-S-phosphate has been synthesized and its enzymatic hydrolysis to cysteamine and orthophosphate demonstrated ( Akerfeldt, 1959, 1960). Earlier, Binkley (1949) demonstrated the enzymatic cleavage of monothiolphosphate to orthophosphate and sulfide. While investigating the cleavage of thiolphosphates with enzymes obtained from Escherichia coli , glucose was found to be a potent inhibitior. Evidence presented in this report suggests that an enzymatic phosphoryl transfer from monothiolphosphate to glucose probably accounts for this inhition.