biostudies-literatureStockbridge RBNIGMS NIH HHS18248-9https://www.ebi.ac.uk/biostudies/studies/S-EPMC2802104biostudies-literatureUnknown131(51)The hydrolysis of simple phosphate monoesters is among the most difficult reactions that are subject to catalysis by enzymes, and it has been suggested that extraction of the substrates from solvent water may contribute to the catalytic effects of phosphohydrolases. Here, we show that the tetrabutylammonium salt of neopentyl phosphate enters wet cyclohexane at concentrations sufficient to allow determination of its rate of hydrolysis. The second-order rate constant for hydrolysis of the phosphomonoester dianion is enhanced approximately 2 x 10(12)-fold by transfer from water to cyclohexane. That rate enhancement arises from an increase in the entropy of activation.Journal of the American Chemical SocietyPhosphate monoester hydrolysis in cyclohexane.PMC2802104GM-18325R01 GM018325-39R37 GM018325R01 GM018325Wolfenden RStockbridge RBfalsePhosphate monoester hydrolysis in cyclohexane.The hydrolysis of simple phosphate monoesters is among the most difficult reactions that are subject to catalysis by enzymes, and it has been suggested that extraction of the substrates from solvent water may contribute to the catalytic effects of phosphohydrolases. Here, we show that the tetrabutylammonium salt of neopentyl phosphate enters wet cyclohexane at concentrations sufficient to allow determination of its rate of hydrolysis. The second-order rate constant for hydrolysis of the phosphomonoester dianion is enhanced approximately 2 x 10(12)-fold by transfer from water to cyclohexane. That rate enhancement arises from an increase in the entropy of activation.2009-01-01T00:00:00Z2009 Dec2025-04-04T07:38:17.434Z2019-03-26T23:28:34ZS-EPMC28021042002814610.1021/ja907967y