EC Number   |
Reaction |
Reference  |
|---|
    5.3.1.8 | D-Mannose 6-phosphate = D-fructose 6-phosphate |
- |
- |
| 5.3.1.8 | D-Mannose 6-phosphate = D-fructose 6-phosphate |
analysis of enzyme-substrate and enzyme-inhibitor complexes by ESI-FTICR mass spectrometry |
660706 |
| 5.3.1.8 | D-Mannose 6-phosphate = D-fructose 6-phosphate |
cis-enediol mechanism |
661100 |
| 5.3.1.8 | D-Mannose 6-phosphate = D-fructose 6-phosphate |
mechanism does not involve trans-enediol. Instead, activity may result from additional space in the active site which permits rotation of the C2-C3 bond |
662267 |
| 5.3.1.8 | D-Mannose 6-phosphate = D-fructose 6-phosphate |
hydride transfer mechanism of a alpha-hydrogen bond between the C1 and C2 positions of substrate. Mechanism involves Zn2+ mediating the movement of a proton between O1 and O2, and the hydrophobic environment formed in part by T278 promoting transfer of a hydride ion |
681498 |
| 5.3.1.8 | D-Mannose 6-phosphate = D-fructose 6-phosphate |
reaction mechanism, overview. Zn2+ binding induces structural order in the loop consisting of residues 50-54. The metal atom appears to play a role in substrate binding and is probably also important for maintaining the architecture of the active site. Isomerization probably follows a cis-enediol mechanism, overall folding pattern of the central catalytic domain, overview |
701472 |
