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pubmed:abstractText |
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.
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