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.
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