EC Number   |
Reaction |
Reference |
|---|
    2.7.6.3 | ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate |
- |
- |
| 2.7.6.3 | ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate |
during its catalytic cycle, the enzyme must assume at least five liganded forms: the apoenzyme form (without either of the substrates), the binary substrate complex with MgATP, the ternary substrate complex (Michaelis complex) with MgATP and 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine, the ternary product complex with AMP and 6-hydroxymethyl-7,8-dihydropterin diphosphate (HPPP), and the binary product complex with HPPP |
737717 |
| 2.7.6.3 | ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate |
in the enzyme mechanism, the assembly of the pterin-binding pocket depends on ATP-dependent conformational changes in the three active site loops |
737836 |
| 2.7.6.3 | ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate |
ordered kinetic mechanism, with Mg2+-dependent ATP binding followed by rapid addition of 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine |
-, 738210 |
