RGD Reference Report - Inactivation of phosphofructokinase by glucagon in rat hepatocytes. - Rat Genome Database

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Inactivation of phosphofructokinase by glucagon in rat hepatocytes.

Authors: Castano, JG  Nieto, A  Feliu, JE 
Citation: Castano JG, etal., J Biol Chem. 1979 Jul 10;254(13):5576-9.
RGD ID: 2301234
Pubmed: PMID:156182   (View Abstract at PubMed)

Kinetic evidence of a time- and dose-dependent inactivation of phosphofructokinase by glucagon in isolated rat hepatocytes is reported. This inactivation, which persists after gel filtration of a cell-free extract on Sephadex G-25 and after 400-fold purification of the enzyme on agarose-ATP, is observed when the enzyme activity is measured at subsaturating concentrations of fructose 6-phosphate, while there is no change in Vmax. Phosphofructokinase inactivation by glucagon parallels the known inactivation of pyruvate kinase L and activation of glycogen phosphorylase alpha. Exogenous cyclic AMP mimics the effect of this hormone. Half-maximal effect for both phosphofructokinase and pyruvate kinase L is caused by a similar dose of glucagon (1 x 10(-10) M). The inactivation of phosphofructokinase by nonsaturating concentration of glucagon is reversed spontaneously within 40 min of incubation and this reversion is accelerated by insulin.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
fructose 6-phosphate metabolic process  IDA 2301234 RGD 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
6-phosphofructokinase activity  IDA 2301234 RGD 
ATP binding  IDA 2301234 RGD 
monosaccharide binding  IDA 2301234 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Pfkl  (phosphofructokinase, liver type)


Additional Information