EC Number   |
Natural Substrates |
|---|
    2.4.1.217 | GDP-glucose + 3-phospho-D-glycerate |
- |
| 2.4.1.217 | GDP-mannose + 3-phospho-D-glycerate |
- |
| 2.4.1.217 | GDP-mannose + 3-phospho-D-glycerate |
2 pathways for mannosylglycerate biosynthesis, a one-step and a two-step pathway, with specialized roles in osmoadaptation and thermoadaptation, the isozyme involved in the two-step pathway is upregulated by osmotic stress, the isozyme involved in the one-step pathway is upregulated by heat stress, regulatory mechanisms, overview |
| 2.4.1.217 | GDP-mannose + 3-phospho-D-glycerate |
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70) |
| 2.4.1.217 | GDP-mannose + 3-phospho-D-glycerate |
the enzyme is involved in synthesis of mannosylglycerate |
| 2.4.1.217 | GDPmannose + 3-phospho-D-glycerate |
involved in a pathway for synthesis of mannosylglycerate |
| 2.4.1.217 | more |
the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold |
| 2.4.1.217 | more |
the bifunctional enzyme catalyzes the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis, enzyme evolution |
| 2.4.1.217 | more |
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate |
| 2.4.1.217 | more |
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview |
