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: PMID:1733780   (View Abstract at PubMed)

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.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Gys2Ratglycogen metabolic process  IDA  RGD 
PyglRatglycogen metabolic process  IDA  RGD 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Gys2Ratalpha-1,4-glucan glucosyltransferase (UDP-glucose donor) activity  IDA  RGD 
PyglRatglycogen phosphorylase activity  IDA  RGD 

Objects Annotated

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


Additional Information