EC |
3.1.3.85 |
Accepted name: |
glucosyl-3-phosphoglycerate phosphatase |
Reaction: |
2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate + H2O = 2-O-(α-D-glucopyranosyl)-D-glycerate + phosphate |
Other name(s): |
GpgP protein |
Systematic name: |
α-D-glucosyl-3-phospho-D-glycerate phosphohydrolase |
Comments: |
The enzyme is involved in biosynthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase. In vivo the enzyme catalyses the dephosphorylation of 2-O-(α-D-mannopyranosyl)-3-phospho-D-glycerate with lower efficiency [1,2]. Divalent metal ions (Mg2+, Mn2+ or Co2+) stimulate activity [1,2]. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
References: |
1. |
Costa, J., Empadinhas, N. and da Costa, M.S. Glucosylglycerate biosynthesis in the deepest lineage of the bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina. J. Bacteriol. 189 (2007) 1648–1654. [DOI] [PMID: 17189358] |
2. |
Costa, J., Empadinhas, N., Goncalves, L., Lamosa, P., Santos, H. and da Costa, M.S. Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii. J. Bacteriol. 188 (2006) 1022–1030. [DOI] [PMID: 16428406] |
3. |
Mendes, V., Maranha, A., Alarico, S., da Costa, M.S. and Empadinhas, N. Mycobacterium tuberculosis Rv2419c, the missing glucosyl-3-phosphoglycerate phosphatase for the second step in methylglucose lipopolysaccharide biosynthesis. Sci. Rep. 1:177 (2011). [DOI] [PMID: 22355692] |
|
[EC 3.1.3.85 created 2011] |
|
|
|
|