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Literature summary for 2.7.7.27 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

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

Inhibitors

Inhibitors Comment Organism Structure
phosphate inhibitor follows hyberbolic kinetics Hordeum vulgare

KM Value [mM]

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

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + alpha-D-glucose 1-phosphate Hordeum vulgare key regulatory enzyme of starch biosynthesis diphosphate + ADP-glucose
-
?

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Hordeum vulgare
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + alpha-D-glucose 1-phosphate
-
Hordeum vulgare diphosphate + ADP-glucose
-
r
ATP + alpha-D-glucose 1-phosphate key regulatory enzyme of starch biosynthesis Hordeum vulgare diphosphate + ADP-glucose
-
?