Escherichia coli AspP activity is enhanced by macromolecular crowding and by both glucose-1,6-bisphosphate and nucleotide-sugars

VIALE, ALEJANDRO MIGUEL; MORAN-ZORZANO M.T.; FRANCISCO MUÑOZ,; ALONSO CASAJÚS, NORA; EYDALLIN, G.; B. ZUGASTI; BAROJA FERNANDEZ, EDURNE; POZUETA ROMERO, JAVIER

Febs Letters

Elsevier

Año: 2007 vol. 581 p. 1035 - 1040

0014-5793

Escherichia coli ADP-sugar pyrophosphatase (AspP) is a ‘‘Nudix’’ hydrolase that catalyzes the hydrolytic breakdown of ADP-glucose linked to glycogen biosynthesis. Moderate increases of AspP activity in the cell are accompanied by significant reductions of the glycogen content. In vitro analyses showed that AspP activity is strongly enhanced by macromolecular crowding and by both glucose-1,6-bisphosphate and nucleotide-sugars, providing a first set of indicative evidences that AspP is a highly regulated enzyme. To our knowledge, AspP is the sole bacterial enzyme described to date which is activated by both G1,6P2 and nucleotide-sugars.ADP-sugar pyrophosphatase (AspP) is a ‘‘Nudix’’ hydrolase that catalyzes the hydrolytic breakdown of ADP-glucose linked to glycogen biosynthesis. Moderate increases of AspP activity in the cell are accompanied by significant reductions of the glycogen content. In vitro analyses showed that AspP activity is strongly enhanced by macromolecular crowding and by both glucose-1,6-bisphosphate and nucleotide-sugars, providing a first set of indicative evidences that AspP is a highly regulated enzyme. To our knowledge, AspP is the sole bacterial enzyme described to date which is activated by both G1,6P2 and nucleotide-sugars.