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Literature summary extracted from
- Dihydroneopterin triphosphate epimerase of Escherichia coli: Purification, genetic cloning, and expression (1997), J. Bacteriol., 179, 949-951.
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.1.99.8 | 14000 | - |
x * 14000, SDS-PAGE | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.99.8 | Escherichia coli | P0AC19 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.99.8 | - |
Escherichia coli |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.1.99.8 | 11 | - |
pH not specified in the publication, temperature not specified in the publication | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.99.8 | 7,8-dihydroneopterin triphosphate | enzyme catalyzes the epimerization at position 2' of dihydroneopterin triphosphate | Escherichia coli | 7,8-dihydromonapterin triphosphate | - |
? |  |
| 5.1.99.8 | additional information | aldolase activity, EC 4.1.2.25, of the enzyme is 10000fold less than the epimerase activity | Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.1.99.8 | ? | x * 14000, SDS-PAGE | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.99.8 | dihydroneopterin triphosphate 2'-epimerase | - |
Escherichia coli |
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