Oxygen chiral phosphate esters stereochemical studies using

Stereochemical Studies Using Oxygen Chiral Phosphate Esters and P-NMR Methods of... 

As noted previously, the stereochemical course of the hydrolysis of a phosphate monoester can be studied only if an oxygen chiral phosphorothioate ester is used a substrate so that an enantiomer of 0-labeled chiral thiophos-... 

These comparative studies constituted the first example of an enzyme-catalyzed hydrolysis reaction whose stereochemical course was unaffected by sulfur substitution. At the time these experiments were performed, the stereochemical courses of the reactions catalyzed by glycerol kinase (83, 84) and by the bacterial adenylate cyclase (85, 86) had already been compared in the laboratories of Knowles and Gerlt, respectively, and these were also found to be unaffected by the sulfur substitution. A number of other comparisons of this type have been made, and in no case were the stereochemical consequences of the reactions studied with chiral phosphate esters and the chiral thiophosphate analogs found to differ. This agreement suggests that the necessary use of oxygen chiral thiophosphate monoesters to study the stereochemical course of phospho-monoesterases will provide pertinent results for ascertaining whether phosphory-lated intermediates are involved in the reaction mechanism. 

---