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Literature summary extracted from

  • Boehlein, S.K.; Shaw, J.R.; Hannah, L.C.; Stewart, J.D.
    Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase (2010), Plant Physiol., 152, 85-95.
    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 D-fructose 6-phosphate allosteric activator Zea mays
2.7.7.27 D-glucose 6-phosphate allosteric activator Zea mays

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.27 R104A large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize Zea mays
2.7.7.27 R107A small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize Zea mays
2.7.7.27 R116A large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize Zea mays
2.7.7.27 R146A large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize Zea mays
2.7.7.27 R340A small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize Zea mays
2.7.7.27 R381A large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize Zea mays
2.7.7.27 R77K small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.27 inorganic phosphate
-
 Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.27 0.12
-
 ATP wild type Zea mays
2.7.7.27 0.13
-
 ATP small subunit mutant R107A Zea mays
2.7.7.27 0.19
-
 ATP large subunit mutant R116A Zea mays
2.7.7.27 0.26
-
 ATP large subunit mutant R381A Zea mays
2.7.7.27 0.36
-
 ATP small subunit mutant R340A Zea mays
2.7.7.27 0.42
-
 ATP large subunit mutant R146A Zea mays
2.7.7.27 1.1
-
 ATP small subunit mutant R77K Zea mays
2.7.7.27 1.4
-
 ATP large subunit mutant R104A 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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.7.27 11
-
 ATP large subunit mutant R104A Zea mays
2.7.7.27 11
-
 ATP large subunit mutant R146A Zea mays
2.7.7.27 11
-
 ATP small subunit mutant R77K Zea mays
2.7.7.27 16
-
 ATP small subunit mutant R340A Zea mays
2.7.7.27 33
-
 ATP large subunit mutant R116A Zea mays
2.7.7.27 69
-
 ATP large subunit mutant R381A Zea mays
2.7.7.27 70
-
 ATP small subunit mutant R107A Zea mays
2.7.7.27 98
-
 ATP wild type 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