EC Number   |
Reaction |
Reference |
|---|
    4.2.1.75 | hydroxymethylbilane = uroporphyrinogen III + H2O |
- |
- |
| 4.2.1.75 | hydroxymethylbilane = uroporphyrinogen III + H2O |
in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, reaction mechanism, does not require acid/base catalysis, active site structure |
649817, 650984 |
| 4.2.1.75 | hydroxymethylbilane = uroporphyrinogen III + H2O |
in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, Tyr166 is essential for catalysis and/or substrate binding |
651309 |
| 4.2.1.75 | hydroxymethylbilane = uroporphyrinogen III + H2O |
reaction mechanism via azafulvene and azofulvene intermediates, the product binds between the two domains and is held in place by a network of hydrogen bonds between the products side chain carboxylates and the proteins main chain amides. Interactions of the product A and B ring carboxylate side chains with both structural domains of U3S appear to dictate the relative orientation of the domains in the closed enzyme conformation and likely remain intact during catalysis. The product C and D rings are less constrained in the structure, consistent with the conformational changes required for the catalytic cyclization with inversion of D ring orientation. A conserved tyrosine residue is potentially positioned to facilitate loss of a hydroxyl from the substrate to initiate the catalytic reaction, overview |
-, 696286 |
| 4.2.1.75 | hydroxymethylbilane = uroporphyrinogen III + H2O |
reaction mechanism, modeling involving Tyr168, overview |
713692 |
| 4.2.1.75 | hydroxymethylbilane = uroporphyrinogen III + H2O |
reaction mechanism, modelling, overview |
699766 |
