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Literature summary for 2.7.7.27 extracted from
- Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli (2001), J. Biol. Chem., 276, 46319-46325.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| D-fructose 1,6-bisphosphate | - |
Escherichia coli |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type and D142E plasmids in Escherichia coli strain BL21(DE3), expression of D142N and D142A plasmids in Escherichia coli strain AC70R1-504 | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D142A | Km values are not significantly different in comparison to the wild-type enzyme, no significant changes for fructose 1,6-bisphosphate activation, Ki value of AMP 3fold increases in comparison to the wild-type enzyme | Escherichia coli |
| D142E | 47fold increase of Km value of glucose 1-phosphate and 11.5fold increase of Km value of ATP in comparison to the wild-type enzyme, activation by fructose 1,6-bisphosphate increases, no significant changes for AMP-inhibition in comparison to the wild-type enzyme | Escherichia coli |
| D142N | Km values are not significantly different in comparison to the wild-type enzyme, Ki value of AMP 25fold increases in comparison to the wild-type enzyme | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| AMP | - |
Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.018 | - |
alpha-D-glucose 1-phosphate | pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes | Escherichia coli | |
| 0.26 | - |
ATP | pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + alpha-D-glucose 1-phosphate | Escherichia coli | major regulated step in the bacterial glycogen biosynthesis pathway | diphosphate + ADP-glucose | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + alpha-D-glucose 1-phosphate | - |
Escherichia coli | diphosphate + ADP-glucose | - |
? | |
| ATP + alpha-D-glucose 1-phosphate | major regulated step in the bacterial glycogen biosynthesis pathway | Escherichia coli | diphosphate + ADP-glucose | - |
? | |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
5 min 80% remaining activity of the wild-type enzyme, 98% remaining activity of the mutant enzyme D142A, 96% remaining activity of the mutant enzyme D142E, 52% remaining activity of the mutant enzyme D142N | Escherichia coli |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.06 | - |
AMP | pH 7.6, 37°C, mutant enzyme D142E | Escherichia coli | |
| 0.13 | - |
AMP | pH 7.6, 37°C, mutant enzyme D142A | Escherichia coli | |
| 1 | - |
AMP | pH 7.6, 37°C, mutant enzyme D142N | Escherichia coli | |
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