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Vanadate inhibits liver fructose-2,6-bisphosphatase.

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Rider, Mark H. [UCL] Bartrons, R. Hue, Louis [UCL]

Vanadate was found to be a reversible non-competitive inhibitor of chicken liver fructose-2,6-bisphosphatase. The inhibition was best observed in the presence of glycerol 2- or 3-phosphate and half-maximal effect was obtained with about 0.15 mM vanadate. Vanadate decreased the extent of phosphorylation of the enzyme (E-P) by fructose 2,6-[2-32P]bisphosphate. This did not result from an increased rate of E-P breakdown, as is the case with phosphoglycerate mutase, an enzyme which shares structural and functional similarity to fructose-2,6-bisphosphate. The data were consistent with the formation of a dead-end transition state analogue of phosphate in the active site. Inhibition of fructose-2,6-bisphosphatase by vanadate offers a likely explanation for the increase in fructose 2,6-bisphosphate concentration brought about by vanadate in isolated rat hepatocytes.

Document type Article de périodique (Journal article) – Journal Article, Research Support, Non-U.S. Gov't
Access type Accès restreint
Publication date 1990
Journal information "European journal of biochemistry / FEBS" - Vol. 190, no. 1, p. 53-6 (1990)
issn 0014-2956
Publication status Publié
Affiliation UCL - MD/BICL - Département de biochimie et de biologie cellulaire
MESH Subject Animals ; Chickens ; Dose-Response Relationship, Drug ; Fructosediphosphates - metabolism ; Glycerophosphates - pharmacology ; Glycolysis - drug effects ; Hexosediphosphates - metabolism ; Kinetics ; Liver - drug effects - enzymology ; Phosphofructokinase-2 ; Phosphoric Monoester Hydrolases - antagonists & inhibitors ; Phosphorylation ; Vanadates - pharmacology
Links
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Bibliographic reference Rider, Mark H. ; Bartrons, R. ; Hue, Louis. Vanadate inhibits liver fructose-2,6-bisphosphatase.. In: European journal of biochemistry / FEBS, Vol. 190, no. 1, p. 53-6 (1990)
Permanent URL http://hdl.handle.net/2078.1/25930