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Literature summary for 3.1.3.10 extracted from
- Functional insights revealed by the crystal structures of Escherichia coli glucose-1-phosphatase (2003), J. Biol. Chem., 278, 31412-31418.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| determination of crystal structure by multiwavelength anomalous dispersion using a tungstate derivate together with the H18A inactive mutant complex structure with D-glucose 1-phosphate at 2.4 A resolution | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.39 | - |
D-glucose 1-phosphate | pH 6.5 | Escherichia coli |  |
| 0.54 | - |
myo-inositol hexakisphosphate | pH 4.5 | Escherichia coli | |
| 1.6 | - |
D-glucose 6-phosphate | - |
Escherichia coli | |
| 2.2 | - |
D-Fructose 1-phosphate | - |
Escherichia coli | |
| 11 | - |
D-ribose 5-phosphate | - |
Escherichia coli | |
| 13 | - |
p-nitrophenyl phosphate | pH 3.5 | Escherichia coli | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | - |
Escherichia coli | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucose 6-phosphate + H2O | Escherichia coli | the enzyme acts as a D-glucose scavenger | D-glucose + phosphate | - |
? | |
| myo-inositol hexakisphosphate + H2O | Escherichia coli | the enzyme is potentially involved in pathogenic inositol phosphate signal transduction pathways via type III secretioin into the host cell | ? + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucose 1-phosphate + H2O | - |
Escherichia coli | D-glucose + phosphate | - |
? | |
| D-glucose 6-phosphate | - |
Escherichia coli | D-glucose + phosphate | - |
? | |
| D-glucose 6-phosphate + H2O | - |
Escherichia coli | D-glucose + phosphate | - |
? | |
| D-glucose 6-phosphate + H2O | the enzyme acts as a D-glucose scavenger | Escherichia coli | D-glucose + phosphate | - |
? | |
| D-ribose 5-phosphate | - |
Escherichia coli | D-ribose + phosphate | - |
? | |
| fructose 1-phosphate | - |
Escherichia coli | fructose + phosphate | - |
? | |
| myo-inositol hexakisphosphate + H2O | - |
Escherichia coli | ? + phosphate | - |
? | |
| myo-inositol hexakisphosphate + H2O | the enzyme is potentially involved in pathogenic inositol phosphate signal transduction pathways via type III secretioin into the host cell | Escherichia coli | ? + phosphate | - |
? | |
| p-nitrophenyl phosphate | - |
Escherichia coli | p-nitrophenol + phosphate | - |
? | |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3 | 6 | p-nitrophenyl phosphate | pH 3.5 | Escherichia coli | |
| 12 | - |
myo-inositol hexakisphosphate | pH 4.5 | Escherichia coli | |
| 42 | - |
D-ribose 5-phosphate | - |
Escherichia coli | |
| 82 | - |
D-glucose 6-phosphate | - |
Escherichia coli | |
| 95 | - |
D-Fructose 1-phosphate | - |
Escherichia coli | |
| 117 | - |
D-glucose 1-phosphate | pH 6.5 | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | - |
p-nitrophenyl phosphate as substrate | Escherichia coli |
| 4.5 | - |
myo-inositol hexakisphophate as substrate | Escherichia coli |
| 6.5 | - |
D-glucose 1-phosphate as substrate | Escherichia coli |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 2.5 | 9.5 | D-glucose 1-phosphate as substrate | Escherichia coli |
| 3 | 7 | myo-inositol hexakisphophate as substrate | Escherichia coli |
| 3 | 6.5 | p-nitrophenyl phosphate as substrate | Escherichia coli |
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