Rabbit muscle fructose-1,6-bisphosphatase is phosphorylated in vivo.

• Authors: Dariusz Rakus , Marek Zarzycki , Andrzej Dzugaj
• Languages of publication: EN

Abstracts

EN

Phosphorylated fructose-1,6-bisphosphatase (FBPase) was isolated from rabbit muscle in an SDS/PAGE homogeneous form. Its dephosphorylation with alkaline phosphatase revealed 2.8 moles of inorganic phosphate per mole of FBPase. The phosphorylated FBPase (P-FBPase) differs from the dephosphorylated enzyme in terms of its kinetic properties like Km and kcat, which are two times higher for the phosphorylated FBPase, and in the affinity for aldolase, which is three times lower for the dephosphorylated enzyme. ephosphorylated FBPase can be a substrate for protein kinase A and the amount of phosphate incorporated per FBPase monomer can reach 2-3 molecules. Since interaction of muscle aldolase with muscle FBPase results in desensitisation of the latter toward AMP inhibition (Rakus & Dzugaj, 2000, Biochem. Biophys. Res. Commun. 275, 611-616), phosphorylation may be considered as a way of muscle FBPase activity regulation.

Keywords

EN

aldolase; muscle; phosphorylation; AMP; fructose-1,6-bisphosphatase

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2003
• Volume: 50
• Issue: 1
• Pages: 115-121

Dates

published

2003

received

2002-10-14

revised

2002-11-11

accepted

2003-02-25

Contributors

author

Dariusz Rakus

• Department of Animal Physiology, Zoological Institute, University of Wrocław, Z. Cybulskiego 30, 50-205 Wrocław, Poland

author

Marek Zarzycki

• Department of Animal Physiology, Zoological Institute, University of Wrocław, Z. Cybulskiego 30, 50-205 Wrocław, Poland

author

Andrzej Dzugaj

• Department of Animal Physiology, Zoological Institute, University of Wrocław, Z. Cybulskiego 30, 50-205 Wrocław, Poland

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