EC Number | General Stability | Organism |
---|---|---|
2.5.1.55 | repeated freezing and thawing causes loss of activity | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.55 | 2-Deoxy-2-fluoro-D-arabinoate-5-phosphate | - |
Escherichia coli | |
2.5.1.55 | Cd2+ | 1 mM | Escherichia coli | |
2.5.1.55 | Cu2+ | 1 mM | Escherichia coli | |
2.5.1.55 | D-ribose 5-phosphate | - |
Escherichia coli | |
2.5.1.55 | Hg2+ | 1 mM | Escherichia coli | |
2.5.1.55 | phosphate | - |
Escherichia coli | |
2.5.1.55 | Zn2+ | 1 mM | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.55 | 0.006 | - |
phosphoenolpyruvate | - |
Escherichia coli | |
2.5.1.55 | 0.02 | - |
D-arabinose 5-phosphate | - |
Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.55 | additional information | no metal requirement | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.5.1.55 | 32000 | - |
3 * 32000, SDS-PAGE | Escherichia coli |
2.5.1.55 | 90000 | - |
gel filtration, non-denaturing PAGE | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.55 | phosphoenolpyruvate + D-arabinose-5-phosphate + H2O | Escherichia coli | the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor | 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate | - |
? | |
2.5.1.55 | phosphoenolpyruvate + D-arabinose-5-phosphate + H2O | Escherichia coli B / ATCC 11303 | the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor | 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.55 | Escherichia coli | - |
- |
- |
2.5.1.55 | Escherichia coli B / ATCC 11303 | - |
- |
- |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.5.1.55 | 3.7 | - |
- |
Escherichia coli |
EC Number | Storage Stability | Organism |
---|---|---|
2.5.1.55 | -20°C, 50% loss of activity after 14 days | Escherichia coli |
2.5.1.55 | -90°C, 0.1 M potassium phosphate buffer, pH 7.2, stable for up to 1 year | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.55 | phosphoenolpyruvate + D-arabinose 5-phosphate | - |
Escherichia coli | 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate | - |
? | |
2.5.1.55 | phosphoenolpyruvate + D-arabinose 5-phosphate | - |
Escherichia coli B / ATCC 11303 | 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate | - |
? | |
2.5.1.55 | phosphoenolpyruvate + D-arabinose-5-phosphate + H2O | the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor | Escherichia coli | 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate | - |
? | |
2.5.1.55 | phosphoenolpyruvate + D-arabinose-5-phosphate + H2O | the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor | Escherichia coli B / ATCC 11303 | 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.55 | trimer | 3 * 32000, SDS-PAGE | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.5.1.55 | 4 | 6 | and a second optimum at pH 9.0 | Escherichia coli |
2.5.1.55 | 9 | - |
and a second optimum at pH 4.0-6.0 | Escherichia coli |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.55 | 1 | - |
D-ribose 5-phosphate | pH 7.3, 37°C | Escherichia coli |