|PROSITE documentation PDOC00158 [for PROSITE entry PS00175]|
Phosphoglycerate mutase (EC 126.96.36.199) (PGAM) and bisphosphoglycerate mutase (EC 188.8.131.52) (BPGM) are structurally related enzymes which catalyze reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate [1,2]. Both enzymes can catalyze three different reactions, although in different proportions:
In mammals, PGAM is a dimeric protein. There are two isoforms of PGAM: the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein. BPGM is a dimeric protein and is found mainly in erythrocytes where it plays a major role in regulating hemoglobin oxygen affinity as a consequence of controlling 2,3-DPG concentration.
The catalytic mechanism of both PGAM and BPGM involves the formation of a phosphohistidine intermediate .
The bifunctional enzyme 6-phosphofructo-2-kinase / fructose-2,6-bisphosphatase (EC 184.108.40.206 and EC 220.127.116.11) (PF2K)  catalyzes both the synthesis and the degradation of fructose-2,6-bisphosphate. PF2K is an important enzyme in the regulation of hepatic carbohydrate metabolism. Like PGAM/BPGM, the fructose-2,6-bisphosphatase reaction involves a phosphohistidine intermediate and the phosphatase domain of PF2K is structurally related to PGAM/BPGM.
The bacterial enzyme α-ribazole-5'-phosphate phosphatase (gene cobC) which is involved in cobalamin biosynthesis also belongs to this family .
We built a signature pattern around the phosphohistidine residue.Note:
Some organisms harbor a form of PGAM independent of 2,3-DPG, this enzyme is not related to the family described above .Last update:
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Le Boulch P., Joulin V., Garel M.-C., Rosa J., Cohen-Solal M.|
|Source||Biochem. Biophys. Res. Commun. 156:874-881(1988).|
|2||Authors||White M.F., Fothergill-Gilmore L.A.|
|Title||Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae.|
|Source||FEBS Lett. 229:383-387(1988).|
|Source||Methods Enzymol. 87:43-51(1982).|
|4||Authors||Bazan J.F., Fletterick R.J., Pilkis S.J.|
|Title||Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 86:9642-9646(1989).|
|5||Authors||O'Toole G.A., Trzebiatowski J.R., Escalante-Semerena J.C.|
|Source||J. Biol. Chem. 269:26503-26511(1994).|
|6||Authors||Grana X., de Lecea L., el-Maghrabi M.R., Urena J.M., Caellas C., Carreras J., Puigdomenech P., Pilkis S.J., Climent F.|
|Title||Cloning and sequencing of a cDNA encoding 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from maize. Possible relationship to the alkaline phosphatase family.|
|Source||J. Biol. Chem. 267:12797-12803(1992).|