Open AccessFructofuranose 2‐phosphate is the product of dephosphorylation of fructose 2,6‐bisphosphate
Author(s) -
PURWIN Claudio,
LAUX Martina,
HOLZER Helmut
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb11473.x
Subject(s) - chemistry , fructose , dephosphorylation , furanose , phosphate , hydrolysis , periodate , fructolysis , stereochemistry , nuclear chemistry , biochemistry , organic chemistry , phosphatase , enzyme , ring (chemistry)
Using comparative ion‐exchange chromatography on Dowex 1X4, the product of dephosphorylation of fructose 2,6‐bisphosphate with purified yeast fructose‐2,6‐bisphosphate 6‐phosphohydrolase, was shown to be identical to the furanose form of fructose 2‐phosphate prepared by chemical synthesis according to Pontis and Fischer [ Biochem. J. 89 , 452–459 (1963)]. As expected for the furanose form of fructose 2‐phosphate, the enzymatically formed product consums 1 mol periodate/mol fructose 2‐phosphate, whereas the chemically synthesized pyranose form consumes 2 mol periodate/mol. In addition, it is shown that the enzymatic product behaves identically to the furanose, not the pyranose, form of fructose 2‐phosphate in hydrolysis of the ester bond at pH 4 and 37°C, as described previously for the chemically synthesized compounds [Pontis and Fischer (1963) vide supra ].