Kinetic studies on the mechanism and regulation of rabbit liver fructose-1,6-bisphosphatase

Feng Liu, Herbert J. Fromm

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Abstract

The interaction of Mg2+, AMP, and fructose 2,6-bisphosphate with respect to rabbit liver fructose-1,6-bisphosphatase was investigated by studying initial-rate kinetics of the system at pH 9.5. A rapid-equilibrium Random Bi Bi mechanism is suggested for the rabbit liver enzyme from the kinetic data. Our kinetic findings indicate that Mg2+ and the inhibitor AMP are mutually exclusive in their binding to fructose-1,6-bisphosphatase. This probably is the mechanism for AMP regulation of fructose-1,6-bisphosphatase and thus, to some extent, gluconeogenesis. A kinetic model for the interaction of these ligands with respect to rabbit liver fructose-1,6-bisphosphatase is presented.

Original languageEnglish (US)
Pages (from-to)7401-7406
Number of pages6
JournalJournal of Biological Chemistry
Volume265
Issue number13
StatePublished - May 5 1990
Externally publishedYes

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Fructose-Bisphosphatase
Liver
Adenosine Monophosphate
Rabbits
Kinetics
Gluconeogenesis
Ligands
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kinetic studies on the mechanism and regulation of rabbit liver fructose-1,6-bisphosphatase. / Liu, Feng; Fromm, Herbert J.

In: Journal of Biological Chemistry, Vol. 265, No. 13, 05.05.1990, p. 7401-7406.

Research output: Contribution to journalArticle

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