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Literature summary for 2.7.7.27 extracted from
- Covalent modification of Escherichia coli ADPglucose synthetase with 8-azido substrate analogs (1986), Arch. Biochem. Biophys., 244, 585-595.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 1,6-Hexanediol bisphosphate | - |
Escherichia coli |  |
| D-fructose 1,6-bisphosphate | - |
Escherichia coli | |
General Stability
| General Stability | Organism |
|---|---|
| the irradiation of enzyme in the presence of 8-N3ATP, fructose 1,6-phosphate and Mg2+ result in the covalent modification accompanying the loss of the enzyme activity | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 8-azaADP-glucose | photoinactivation, competitive inhibition, ADP-glucose and ATP protects | Escherichia coli | |
| 8-azaATP | photoinactivation, competitive inhibition, 0.5 mol/mol enzyme subunit for complete inactivation, ADP-glucose and ATP protects | Escherichia coli | |
| 8-N3ADPglucose | - |
Escherichia coli | |
| 8-N3ATP | - |
Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.76 | - |
8-azaATP | pH 8.5, 37°C, influence of activators on Km | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| side-chain modification | covalent modification with 8-azaATP and 8-azaADP-glucose accompanies irreversible loss of the enzyme catalytic activity, in the presence of light | Escherichia coli |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 8-azaATP + alpha-D-glucose 1-phosphate | the photoaffinity labeling agent is used as a site specific probe of enzyme | Escherichia coli | diphosphate + 8-azaADP-glucose | reverse reaction is biphasic | r | |
| ATP + alpha-D-glucose 1-phosphate | - |
Escherichia coli | diphosphate + ADP-glucose | - |
? | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.25 | - |
8-N3ADPglucose | pH 8.5, 37°C | Escherichia coli | |
| 1.25 | - |
8-N3ATP | pH 8.5, 37°C | Escherichia coli | |
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