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Literature summary extracted from
- Purification, cloning, and functional expression of dihydroneopterin triphosphate 2'-epimerase from Escherichia coli (1997), J. Biol. Chem., 272, 15323-15328.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.99.7 | DNA and amino acid sequence determination and analysis | Escherichia coli |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.1.99.7 | 13700 | - |
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation | Escherichia coli |
| 5.1.99.7 | 13993 | - |
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation | Escherichia coli |
| 5.1.99.7 | 82600 | - |
gel filtration | Escherichia coli |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.99.7 | 7,8-dihydroneopterin 3'-triphosphate | Escherichia coli | - |
7,8-dihydromonapterin 3'-triphosphate | - |
r |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.99.7 | Escherichia coli | P0AC19 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.99.7 | native enzyme 954fold by ammonium sulfate fractionation, Cibacron blue 3GA affinity chromatography, hydrophobic interaction chromatography, methotrexate affinity chromatography, and ge filtration, to homogeneity | Escherichia coli |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.1.99.7 | 505 | - |
purified native enzyme, substrate 7,8-dihydroneopterin 3'-triphosphate, pH 6.2, 50°C | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.99.7 | 7,8-dihydroneopterin 3'-triphosphate | - |
Escherichia coli | 7,8-dihydromonapterin 3'-triphosphate | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.1.99.7 | homohexamer | 6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.99.7 | H2NTP 2'-epimerase | - |
Escherichia coli |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.99.7 | 50 | - |
assay at | Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.99.7 | 6.2 | - |
assay at | Escherichia coli |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.1.99.7 | metabolism | in Escherichia coli, L-monapterin is made from dihydromonapterin triphosphate after successive dephosphorylation and oxidation. Dihydromonapterin triphosphate is formed by an epimerase acting on C2' carbon of dihydroneopterin triphosphate, which is made from GTP by GTP cyclohydrolase I (EC 3.5.4.16) | Escherichia coli |
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