The enzyme mannosyl-3-phosphoglycerate phosphatase[1] (EC 3.1.3.70) catalyzes the reaction
| mannosyl-3-phosphoglycerate phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.70 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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- 2-O-(α-D-mannosyl)-3-phosphoglycerate + H2O = 2-O-(α-D-mannosyl)-D-glycerate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 2-O-(α-D-mannosyl)-3-phosphoglycerate phosphohydrolase.
Structural studies
editAs of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1WZC and 1XVI.
References
edit- ^ Empadinhas N, Marugg JD, Borges N, Santos H, da Costa MS (2001). "Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes". J. Biol. Chem. 276 (47): 43580–8. doi:10.1074/jbc.M108054200. PMID 11562374.
