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- W2029642263 abstract "Evidence is presented that highly purified preparations of d-fructose-1,6-diphosphatase exhibit β-glycerophosphatase activity. Circumstantial evidence suggests that the β-glycerophosphatase activity shares its active site with the neutral (pH 6.5) activity toward fructose 1,6-diphosphate. This evidence includes the correlation of β-glycerophosphatase activity with the neutral activity in six preparations, and similar responses of the two activities to the presence of 5'-AMP and to treatment with nagarse. In addition, fructose 1,6-diphosphate was found to inhibit glycerol release from β-glycerophosphate, while β-glycerophosphate competitively inhibited fructose 1,6-diphosphate hydrolysis at pH 9.0, indicating that the β-glycerophosphate activity site is functionally identical to the alkaline activity site. It is concluded that purified d-fructose-1,6-diphosphatase has three definable activities—neutral activity with fructose 1,6-diphosphate, alkaline activity with fructose 1,6-diphosphate, and the ability to dephosphorylate β-glycerophosphate. Evidence is presented that these three activities share a common active site." @default.
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- W2029642263 date "1971-09-01" @default.
- W2029642263 modified "2023-09-27" @default.
- W2029642263 title "Bovine hepatic fructose 1,6-diphosphatase: β-glycerophosphate hydrolysis-evidence for a shared active site" @default.
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- W2029642263 doi "https://doi.org/10.1016/s0003-9861(71)80050-4" @default.
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