RGD Reference Report - Glucose has to be phosphorylated to activate glycogen synthase, but not to inactivate glycogen phosphorylase in hepatocytes. - Rat Genome Database

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Glucose has to be phosphorylated to activate glycogen synthase, but not to inactivate glycogen phosphorylase in hepatocytes.

Authors: Carabaza, A  Ciudad, CJ  Baque, S  Guinovart, JJ 
Citation: Carabaza A, etal., FEBS Lett. 1992 Jan 20;296(2):211-4.
RGD ID: 2304117
Pubmed: (View Article at PubMed) PMID:1733780

2-Deoxyglucose and 5-thioglucose, in the same fashion as glucose, cause the inactivation of the rat hepatocyte glycogen phosphorylase and the activation of glycogen synthase. However, 6-deoxyglucose and 1,5-anhydroglucitol inactivate phosphorylase without increasing the activation state of glycogen synthase. With 3-O-methylglucose no changes in the activity of these enzymes occurred. These results prove that while glucose is the molecule that triggers the inactivation of phosphorylase, glucose 6-phosphate is the signal for glucose synthase activation and that a metabolite control of the activation state of glycogen synthase is operative in hepatocytes.

Annotation

Gene Ontology Annotations    

Biological Process

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Gys2  (glycogen synthase 2)
Pygl  (glycogen phosphorylase L)


Additional Information