EC Number   |
Reaction |
Reference |
|---|
    2.4.1.217 | GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate |
- |
- |
| 2.4.1.217 | GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate |
front-face SNi-like reaction mechanism, detailed overview. The binding of GDP-mannose:Mn2+ to the enzyme from Rhodothermus marinus induces significant conformational changes in the flexible loop. In particular, Tyr220 plays a pivotal role both in D-glycerate binding and in catalysis: it is reoriented towards the pocket interior and either interacts with the a phosphate of GDP-mannose |
736076 |
| 2.4.1.217 | GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate |
front-face SNi-like reaction mechanism, overview |
-, 736076 |
| 2.4.1.217 | GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate |
the enzyme is bifunctional exhibiting both mannosyl-3-phosphoglycerate synthase, EC 2.4.1.217, and mannosyl-3-phosphoglycerate phosphatase, EC 3.1.3.70, activities, catalyzing the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis |
659043 |
