Unambiguous Stereochemical Course of Rabbit Liver Fructose Bisphosphatase Hydrolysis

Jubrail F. Rahil; Paul L. Domanico; Stephen J. Benkovic

doi:10.1021/bi00328a009

Unambiguous Stereochemical Course of Rabbit Liver Fructose Bisphosphatase Hydrolysis

Jubrail F. Rahil, Paul L. Domanico, Stephen J. Benkovic

Chemistry

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21 Scopus citations

Abstract

The stereochemical course of rabbit liver fructose bisphosphatase (EC 3.1.3.11) was determined by hydrolyzing the substrate analogue (SP)-[l-18O]fructose 1-phosphorothioate 6-phosphate in H217O, incorporating the chiral, inorganic phosphorothioate product into adenosine 5'-O-(2-thiotriphosphate) (ATPβS), and analyzing the isotopic distribution of 18O in ATPβS by 31P NMR. The result indicates that the 1-phosphoryl group is transferred with inversion of configuration. A series of single-turnover experiments ruled out an acyl phosphate intermediate in the hydrolysis. Consequently, fructose bisphosphatase catalyzes the hydrolysis of fructose 1,6-bisphosphate via a direct transfer of the phosphoryl moiety to water.

Original language	English (US)
Pages (from-to)	1623-1628
Number of pages	6
Journal	Biochemistry
Volume	24
Issue number	7
DOIs	https://doi.org/10.1021/bi00328a009
State	Published - Mar 1 1985

All Science Journal Classification (ASJC) codes

Biochemistry

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10.1021/bi00328a009

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title = "Unambiguous Stereochemical Course of Rabbit Liver Fructose Bisphosphatase Hydrolysis",

abstract = "The stereochemical course of rabbit liver fructose bisphosphatase (EC 3.1.3.11) was determined by hydrolyzing the substrate analogue (SP)-[l-18O]fructose 1-phosphorothioate 6-phosphate in H217O, incorporating the chiral, inorganic phosphorothioate product into adenosine 5'-O-(2-thiotriphosphate) (ATPβS), and analyzing the isotopic distribution of 18O in ATPβS by 31P NMR. The result indicates that the 1-phosphoryl group is transferred with inversion of configuration. A series of single-turnover experiments ruled out an acyl phosphate intermediate in the hydrolysis. Consequently, fructose bisphosphatase catalyzes the hydrolysis of fructose 1,6-bisphosphate via a direct transfer of the phosphoryl moiety to water.",

author = "Rahil, {Jubrail F.} and Domanico, {Paul L.} and Benkovic, {Stephen J.}",

year = "1985",

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T1 - Unambiguous Stereochemical Course of Rabbit Liver Fructose Bisphosphatase Hydrolysis

AU - Rahil, Jubrail F.

AU - Domanico, Paul L.

AU - Benkovic, Stephen J.

PY - 1985/3/1

Y1 - 1985/3/1

N2 - The stereochemical course of rabbit liver fructose bisphosphatase (EC 3.1.3.11) was determined by hydrolyzing the substrate analogue (SP)-[l-18O]fructose 1-phosphorothioate 6-phosphate in H217O, incorporating the chiral, inorganic phosphorothioate product into adenosine 5'-O-(2-thiotriphosphate) (ATPβS), and analyzing the isotopic distribution of 18O in ATPβS by 31P NMR. The result indicates that the 1-phosphoryl group is transferred with inversion of configuration. A series of single-turnover experiments ruled out an acyl phosphate intermediate in the hydrolysis. Consequently, fructose bisphosphatase catalyzes the hydrolysis of fructose 1,6-bisphosphate via a direct transfer of the phosphoryl moiety to water.

AB - The stereochemical course of rabbit liver fructose bisphosphatase (EC 3.1.3.11) was determined by hydrolyzing the substrate analogue (SP)-[l-18O]fructose 1-phosphorothioate 6-phosphate in H217O, incorporating the chiral, inorganic phosphorothioate product into adenosine 5'-O-(2-thiotriphosphate) (ATPβS), and analyzing the isotopic distribution of 18O in ATPβS by 31P NMR. The result indicates that the 1-phosphoryl group is transferred with inversion of configuration. A series of single-turnover experiments ruled out an acyl phosphate intermediate in the hydrolysis. Consequently, fructose bisphosphatase catalyzes the hydrolysis of fructose 1,6-bisphosphate via a direct transfer of the phosphoryl moiety to water.

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Unambiguous Stereochemical Course of Rabbit Liver Fructose Bisphosphatase Hydrolysis

Abstract

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