Any feedback?
Literature summary for 2.7.7.27 extracted from
- Studies of the kinetic mechanism of maize endosperm ADP-glucose pyrophosphorylase uncovered complex regulatory properties (2010), Plant Physiol., 152, 1056-1064.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 3-phosphoglycerate | - |
Zea mays |  |
| ADP-glucose | in the absence of 3-phosphoglycerate, ADP-glucose stimulates catalytic acitvity, acting as a feedback product activator | Zea mays | |
| phosphate | enhances AGPase activity al low substrate concentations | Zea mays | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| for expression in Escherichia coli AC70R1-504 cells | Zea mays |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ADP-glucose | in the presence of 3-phosphoglycerate, ADP-glucose is a competitve inhibitor with respect to ATP | Zea mays | |
| inorganic phosphate | inhibitor in the absence of 3-phosphoglycerate and high substrate levels | 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 |
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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
