Reciprocal regulation of fructose 1,6-bisphosphatase and phosphofructokinase by fructose 2,6-bisphosphate in swine kidney

Muniyappa, K. ; Leibach, Fredrich H. ; Mendicino, Joseph (1983) Reciprocal regulation of fructose 1,6-bisphosphatase and phosphofructokinase by fructose 2,6-bisphosphate in swine kidney Life Sciences, 32 (3). pp. 271-278. ISSN 0024-3205

Full text not available from this repository.

Official URL: http://linkinghub.elsevier.com/retrieve/pii/002432...

Related URL: http://dx.doi.org/10.1016/0024-3205(83)90040-1

Abstract

The effect of fructose 2,6-P2, AMP and substrates on the coordinate inhibition of FBPase and activation of PFK in swine kidney has been examined. Fructose 2,6-P2 inhibits the activity of FBPase and stimulates the activity of PFK in the presence of inhibitory concentrations of ATP. Under similar conditions 2.2 μM fructose 2,6-P2 was required for 50% inhibition of FBPase and 0.04 μM fructose 2,6-P2 restored 50% of the activity of PFK. Fructose 2,6-P2 also enhanced the allosteric activation of PFK by AMP and it increased the extent of inhibition of FBPase by AMP. Fructose 2,6-P2, AMP and fructose 6-P act cooperatively to stimulate the activity of PFK whereas the same latter two effectors and fructose 1,6-P2 inhibit the activity of FBPase. Taken collectively, these results suggest that an increase in the intracellular level of fructose 2,6-P2 during gluconeogenesis could effectively overcome the inhibition of PFK by ATP and simulataneously inactivate FBPase. When the level of fructose 2,6-P2 is low, a glycolytic state would be restored, since under these conditions PFK would be inhibited by ATP and FBPase would be active.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:22457
Deposited On:25 Nov 2010 14:01
Last Modified:08 Jun 2011 08:34

Repository Staff Only: item control page