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.
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