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Literature summary for 2.7.7.27 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

Activating Compound Comment Organism Structure
3-phosphoglycerate
-
Zea mays
D-fructose 6-phosphate allosteric activator Zea mays
D-glucose 6-phosphate allosteric activator Zea mays

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
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
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

Inhibitors Comment Organism Structure
inorganic phosphate
-
Zea mays

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Zea mays

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
endosperm
-
Zea mays
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
ADP-glucose pyrophosphorylase
-
Zea mays
AGPase
-
Zea mays

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
Zea mays

General Information

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