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Literature summary for 2.7.7.27 extracted from
- Heat stability and allosteric properties of the maize endosperm ADP-glucose pyrophosphorylase are intimately intertwined (2008), Plant Physiol., 146, 289-299.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 3-phosphoglycerate | - |
Zea mays |  |
| fructose-6-phosphate | - |
Zea mays | |
| Fruf-beta-(2->1)-6-O-P-Glcp | - |
Zea mays | |
| glucose-6-phosphate | - |
Zea mays | |
| glycerol phosphate | - |
Zea mays | |
| additional information | no activation by D-6-phosphogluconic acid, ribose 1,5-diphosphate, erythrose 4-phosphate, or methyl phosphate at 20 mM | Zea mays | |
| phosphoenolpyruvate | - |
Zea mays | |
| ribose-5-phosphate | - |
Zea mays | |
General Stability
| General Stability | Organism |
|---|---|
| phosphate, in the absence of 3-PGA, stabilizes endosperm AGPase | Zea mays |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| phosphate | phosphate binds tightly to the endosperm AGPase, but does not inhibit catalytic activity, it acts by displacing bound activators and returning the enzyme to its activity in their absence. Phosphate, in the absence of 3-PGA, also stabilizes maize endosperm AGPase | Zea mays | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | ordered kinetic mechanism, regulation of AGPase by effectors, detailed overview | 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 | AGPase, a key regulatory enzyme in starch biosynthesis, is highly regulated, effects of substrates, detailed overview | ADP-D-glucose + diphosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| 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 | ADP-D-glucose + diphosphate | - |
r | |
| ATP + alpha-D-glucose 1-phosphate | AGPase, a key regulatory enzyme in starch biosynthesis, is highly regulated, effects of substrates, detailed overview | Zea mays | ADP-D-glucose + diphosphate | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the enzyme exists in two forms that have significantly different stabilities and do not interconvert rapidly | Zea mays |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADP-glucose pyrophosphorylase | - |
Zea mays |
| AGPase | - |
Zea mays |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
ATP and ADP-Glc, but not Glc-1-P and diphosphate, protect AGPase from thermal inactivation, 3-PGA acts synergistically, overview | Zea mays |
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Release 2023.1 (January 2023)
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