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Literature summary for 5.4.2.6 extracted from
- Theoretical investigation of the enzymatic phosphoryl transfer of beta-phosphoglucomutase: revisiting both steps of the catalytic cycle (2012), J. Mol. Model., 18, 3169-3179.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Lactococcus lactis |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-D-Glucose 1-phosphate | Lactococcus lactis | - |
beta-D-Glucose 6-phosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lactococcus lactis | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate | reaction mechanism of the phosphoryl transfer starting from the bisphosphate intermediate beta-D-glucose-1,6-(bis)phosphate in both directions of the reversible reaction, overview. The calculated energy barrier of the reaction for the beta-D-glucose 1-phosphate to beta-D-glucose 1,6-diphosphate step is only slightly higher than for the beta-G1,6diP to beta-G6P step. Residues Ser114 and Lys145 and Mg2+ play important roles in stabilizing the large negative charge on the phosphate through strong coordination with the phosphate oxygens and guiding the phosphate group throughout the catalytic process | Lactococcus lactis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-D-Glucose 1-phosphate | - |
Lactococcus lactis | beta-D-Glucose 6-phosphate | - |
r | |
| beta-D-Glucose 1-phosphate | via stabile intermediate beta-D-glucose-1,6-(bis)phosphate | Lactococcus lactis | beta-D-Glucose 6-phosphate | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta-PGM | - |
Lactococcus lactis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | reaction mechanism analysis by docking techniques and QM/MM theoretical method, overview. Residues Ser114 and Lys145 and Mg2+ play important roles in stabilizing the large negative charge on the phosphate through strong coordination with the phosphate oxygens and guiding the phosphate group throughout the catalytic process | Lactococcus lactis |
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