EC Number   |
Reaction |
Reference |
|---|
    5.4.2.11 | 2-phospho-D-glycerate = 3-phospho-D-glycerate |
mechanism of BPGM begins with an unphosphorylated enzyme, the active site histidine of which performs a nucleophilic SN2 attack on the 1,3-bisphosphoglycerate substrate to produce phosphohistidine and 3-phosphoglycerate. The 2'-hydroxyl group then performs a second nucleophilic attack that transfers the phosphate from the active site histidine to the substrate, forming 2,3-bisphosphoglycerate |
-, 726607 |
| 5.4.2.11 | 2-phospho-D-glycerate = 3-phospho-D-glycerate |
mechanism: after the active site His-8 is phosphorylated by the cofactor 2,3-diphosphoglycerate a substrate molecule binds. Subsequently a phospho-transfer takes place via a ping-pong-mechanism. After release of the product the enzyme remains phosphorylated and catalytically competent |
3231 |
| 5.4.2.11 | 2-phospho-D-glycerate = 3-phospho-D-glycerate |
overall reaction |
- |
| 5.4.2.11 | 2-phospho-D-glycerate = 3-phospho-D-glycerate |
ping-pong mechanism via a phosphorylated His-intermediate |
3240 |
| 5.4.2.11 | 2-phospho-D-glycerate = 3-phospho-D-glycerate |
ping-pong or phosphoenzyme mechanism |
661261 |
| 5.4.2.11 | [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-Ntau-phospho-L-histidine + 2/3-phospho-D-glycerate |
(1a) |
- |
| 5.4.2.11 | [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-Ntau-phospho-L-histidine + 3-phospho-D-glycerate |
- |
- |
| 5.4.2.11 | [enzyme]-Ntau-phospho-L-histidine + 2-phospho-D-glycerate = [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate |
(1b) |
- |
| 5.4.2.11 | [enzyme]-Ntau-phospho-L-histidine + 2/3-bisphospho-D-glycerate = [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate |
(1d) |
- |
