Unambiguous Stereochemical Course of Rabbit Liver Fructose Bisphosphatase Hydrolysis

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

Research output: Contribution to journalArticle

20 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1623-1628
Number of pages6
JournalBiochemistry
Volume24
Issue number7
DOIs
StatePublished - Mar 1 1985

Fingerprint

Fructose-Bisphosphatase
Liver
Hydrolysis
Phosphates
Rabbits
Fructose
Nuclear magnetic resonance
Water
Substrates
Experiments
fructose-1,6-diphosphate
adenosine 5'-O-(2-thiotriphosphate)

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Rahil, Jubrail F. ; Domanico, Paul L. ; Benkovic, Stephen J. / Unambiguous Stereochemical Course of Rabbit Liver Fructose Bisphosphatase Hydrolysis. In: Biochemistry. 1985 ; Vol. 24, No. 7. pp. 1623-1628.
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Unambiguous Stereochemical Course of Rabbit Liver Fructose Bisphosphatase Hydrolysis. / Rahil, Jubrail F.; Domanico, Paul L.; Benkovic, Stephen J.

In: Biochemistry, Vol. 24, No. 7, 01.03.1985, p. 1623-1628.

Research output: Contribution to journalArticle

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