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Literature summary extracted from

  • Kleczkowski, L.A.
    Is leaf ADP-glucose pyrophosphorylase an allosteric enzyme? (2000), Biochim. Biophys. Acta, 1476, 103-108.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.27 3-phosphoglycerate activator follows hyberbolic kinetic Hordeum vulgare

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.27 phosphate inhibitor follows hyberbolic kinetics Hordeum vulgare

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.27 0.08
-
 ATP pH 8.0, in presence of 2.5 mM 3-phosphoglycerate Hordeum vulgare
2.7.7.27 0.11
-
 alpha-D-glucose 1-phosphate pH 8.0, in presence of 2.5 mM 3-phosphoglycerate Hordeum vulgare
2.7.7.27 0.33
-
 alpha-D-glucose 1-phosphate pH 8.0, in absence of 3-phosphoglycerate Hordeum vulgare
2.7.7.27 0.9
-
 ATP pH 8.0, in absence of 3-phosphoglycerate Hordeum vulgare

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.27 chloroplast stroma
-
 Hordeum vulgare 9570
-

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 Hordeum vulgare key regulatory enzyme of starch biosynthesis diphosphate + ADP-glucose
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.27 Hordeum vulgare
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.7.27 leaf
-
 Hordeum vulgare
-

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
-
 Hordeum vulgare diphosphate + ADP-glucose
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate key regulatory enzyme of starch biosynthesis Hordeum vulgare diphosphate + ADP-glucose
-
 ?