Purification and properties of the adenosine diphosphoglucose: glycogen transglucosylase of Pasteurella pseudotuberculosis.

Abstract	The enzyme which catalyzes the transfer of glucosyl residues from adenosine diphospho(ADP)-glucose to glycogen has been partially purified from extracts of Pasteurella pseudotuberculosis. In contrast to other glycogen synthetases of this type, guanosine diphospho-glucose had about 5% of the activity of ADP-glucose as a glucosyl donor. Some other properties of the enzyme are described and compared to other bacterial glycogen synthetases.
Authors	D N Dietzler, J L Strominger
Journal	Journal of bacteriology (J Bacteriol) Vol. 113 Issue 2 Pg. 946-52 (Feb 1973) ISSN: 0021-9193 [Print] United States
PMID	4632326 (Publication Type: Journal Article)
Chemical References	Carbon Isotopes Chelating Agents Metals Nucleotides Polysaccharides Sulfhydryl Reagents Adenosine Diphosphate Glycogen Glucosyltransferases Glycogen Synthase Glucose Ammonium Sulfate
Topics	Adenosine Diphosphate Ammonium Sulfate Carbon Isotopes Cell-Free System Chelating Agents (pharmacology) Chemical Precipitation Chromatography Chromatography, Gel Electron Transport Glucose (metabolism) Glucosyltransferases Glycogen (biosynthesis) Glycogen Synthase (antagonists & inhibitors, isolation & purification, metabolism) Hydrogen-Ion Concentration Metals (pharmacology) Nucleotides (metabolism, pharmacology) Pasteurella (enzymology) Polysaccharides (metabolism) Sulfhydryl Reagents (pharmacology)

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