EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  5.1.99.8 | 7,8-dihydromonapterin |
- |
Escherichia coli |
7,8-dihydroneopterin |
- |
? |
| 5.1.99.8 | 7,8-dihydroneopterin |
- |
Solanum lycopersicum |
7,8-dihydromonapterin |
- |
? |
| 5.1.99.8 | 7,8-dihydroneopterin |
- |
Arabidopsis thaliana |
7,8-dihydromonapterin |
- |
? |
| 5.1.99.8 | 7,8-dihydroneopterin |
- |
Staphylococcus aureus |
7,8-dihydromonapterin |
- |
? |
| 5.1.99.8 | 7,8-dihydroneopterin |
- |
Escherichia coli |
7,8-dihydromonapterin |
- |
r |
| 5.1.99.8 | 7,8-dihydroneopterin triphosphate |
- |
Escherichia coli |
7,8-dihydromonapterin triphosphate |
- |
r |
| 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 | more |
aldolase activity, EC 4.1.2.25, of the enzyme is 10000fold less than the epimerase activity |
Escherichia coli |
? |
- |
? |
| 5.1.99.8 | more |
catalyzes the epimerization of carbon 2' in the triphosphates of dihydroneopterin and dihydromonapterin. The enzyme can also catalyze the cleavage of the position 6 side chain of several pteridine derivatives at a slow rate |
Escherichia coli |
? |
- |
? |
| 5.1.99.8 | more |
enzyme catalyzes both the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin, reaction of EC 4.1.2.25, and the epimerization of 7,8-dihydroneopterin to 7,8-dihydromonapterin |
Staphylococcus aureus |
? |
- |
? |
