Literature summary for 2.7.7.27 extracted from

Bejar, C.M.; Ballicora, M.A.; Gomez-Casati, D.F.; Iglesias, A.A.; Preiss, J.
The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains (2004), FEBS Lett., 573, 99-104.

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Activating Compound

Activating Compound	Comment	Organism	Structure
D-fructose 1,6-bisphosphate	-	Escherichia coli
additional information	ADP-glucose diphosphorylase comprises two domains with a strong interaction between them. That interaction is important for allosteric properties and structural stability	Escherichia coli
phosphoenolpyruvate	-	Escherichia coli
pyridoxal 5'-phosphate	-	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
C-terminal truncated enzyme forms, expression in Escherichia coli	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
AMP	-	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
C-terminal truncated enzyme forms	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ADP-glucose pyrophosphorylase	-	Escherichia coli

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Release 2023.1 (January 2023)