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Literature summary for 5.3.1.8 extracted from
- Computational study of human phosphomannose isomerase: Insights from homology modeling and molecular dynamics simulation of enzyme bound substrate (2006), J. Mol. Graph. Model., 25, 289-295.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| homology modeling of structure and refinement by energy minimization and molecular dynamics | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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 | Homo sapiens |
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Release 2023.1 (January 2023)
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