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 (Comment) | Organism |
---|---|
for expression in Escherichia coli AC70R1-504 cells | Zea mays |
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 | Comment | Organism | Structure |
---|---|---|---|
inorganic phosphate | - |
Zea mays |
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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Zea mays |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Zea mays |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
endosperm | - |
Zea mays | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + alpha-D-glucose 1-phosphate | - |
Zea mays | diphosphate + ADP-glucose | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterotetramer | containing two small and two large subunits | Zea mays |
Synonyms | Comment | Organism |
---|---|---|
ADP-glucose pyrophosphorylase | - |
Zea mays |
AGPase | - |
Zea mays |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
activity assay | Zea mays |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
activity assay | Zea mays |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Zea mays |
General Information | Comment | Organism |
---|---|---|
physiological function | ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in starch biosynthesis | Zea mays |