Mannosyl-3-phosphoglycerate phosphatase
| mannosyl-3-phosphoglycerate phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 / EGO | ||||||||
| |||||||||
In enzymology, a mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70) is an enzyme that catalyzes the chemical reaction
- 2(alpha-D-mannosyl)-3-phosphoglycerate + H2O 2(alpha-D-mannosyl)-D-glycerate + phosphate
Thus, the two substrates of this enzyme are 2(alpha-D-mannosyl)-3-phosphoglycerate and H2O, whereas its two products are 2(alpha-D-mannosyl)-D-glycerate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is alpha-D-mannosyl-3-phosphoglycerate phosphohydrolase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1WZC and 1XVI.
References
- 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.
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