Literature summary for 2.7.7.27 extracted from

Kaddis, J.; Zurita, C.; Moran, J.; Borra, M.; Polder, N.; Meyer, C.R.; Gomez, F.A.
Estimation of binding constants for the substrate and activator of Rhodobacter sphaeroides adenosine 5'-diphosphate-glucose pyrophosphorylase using affinity capillary electrophoresis (2004), Anal. Biochem., 327, 252-260.

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Activating Compound

Activating Compound	Comment	Organism	Structure
fructose 6-phosphate	wild-type enzyme is activated, mutant enzyme R33A is insensitive to activation	Cereibacter sphaeroides

Protein Variants

Protein Variants	Comment	Organism
R22A	about 15fold decrease in apparent affinity for fructose 6-phosphate compared to that of wild-type	Cereibacter sphaeroides
R33A	mutant enzyme is insensitive to activation by fructose 6-phosphate	Cereibacter sphaeroides
R8A	mutant enzyme exhibits reduced fold-activation by fructose 6-phosphate compared to that of wild-type but increased apparent affinity for ATP in the presence of fructose 6-phosphate	Cereibacter sphaeroides

Organism

Organism	UniProt	Comment	Textmining
Cereibacter sphaeroides	-	-	-

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Release 2023.1 (January 2023)