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Literature summary extracted from

  • Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Hannah, L.C.
    Studies of the kinetic mechanism of maize endosperm ADP-glucose pyrophosphorylase uncovered complex regulatory properties (2010), Plant Physiol., 152, 1056-1064.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.27 3-phosphoglycerate
-
Zea mays
2.7.7.27 ADP-glucose in the absence of 3-phosphoglycerate, ADP-glucose stimulates catalytic acitvity, acting as a feedback product activator Zea mays
2.7.7.27 phosphate enhances AGPase activity al low substrate concentations Zea mays

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.27 for expression in Escherichia coli AC70R1-504 cells Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.27 ADP-glucose in the presence of 3-phosphoglycerate, ADP-glucose is a competitve inhibitor with respect to ATP Zea mays
2.7.7.27 inorganic phosphate inhibitor in the absence of 3-phosphoglycerate and high substrate levels Zea mays

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.27 Mg2+
-
Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.27 ATP + alpha-D-glucose 1-phosphate Zea mays
-
diphosphate + ADP-glucose
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.27 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.27
-
Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.7.27 endosperm
-
Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.27 ATP + alpha-D-glucose 1-phosphate
-
Zea mays diphosphate + ADP-glucose
-
?

Subunits

EC Number Subunits Comment Organism
2.7.7.27 heterotetramer containing two small and two large subunits Zea mays

Synonyms

EC Number Synonyms Comment Organism
2.7.7.27 ADP-glucose pyrophosphorylase
-
Zea mays
2.7.7.27 AGPase
-
Zea mays

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.27 37
-
activity assay Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.27 7.4
-
activity assay Zea mays

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.7.27 ATP
-
Zea mays

General Information

EC Number General Information Comment Organism
2.7.7.27 physiological function ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in starch biosynthesis Zea mays