Reaction: 2-phospho-D-glycerate = 3-phospho-D-glycerate
Other name(s): phosphoglycerate phosphomutase; phosphoglyceromutase; glycerate phosphomutase (diphosphoglycerate cofactor); monophosphoglycerate mutase; monophosphoglyceromutase; diphosphoglycomutase; diphosphoglycerate mutase; bisphosphoglyceromutase; GriP mutase; MPGM; PGA mutase; PGAM-i; PGAM; PGAM-d; PGM
Systematic name: D-phosphoglycerate 2,3-phosphomutase
Comments: The enzymes from mammals and from yeast are phosphorylated by (2R)-2,3-bis-phosphoglycerate, which is also an intermediate (see introduction to section EC 5.4.2). With the rabbit muscle enzyme, dissociation of bisphosphate from the enzyme is much slower than the overall isomerization. These enzymes also catalyse, slowly, the reactions of EC 220.127.116.11 bisphosphoglycerate mutase; they were formerly listed as EC 18.104.22.168. Enzymes from wheat, rice, insects and some fungi, however, have maximum activity in the absence of 2,3-bisphosphoglycerate, and were formerly listed under the present number as phosphoglycerate phosphomutase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9032-62-6
1. Grisolia, S. Phosphoglyceric acid mutase. Methods Enzymol. 5 (1962) 236-242.
2. Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases, in Boyer, P.D. (Ed.), The Enzymes, 3rd edn., vol. 6, Academic Press, New York , 1972, pp. 407-477.
3. Rose, Z.B. The enzymology of 2,3-bisphosphoglycerate. Adv. Enzymol. Relat. Areas Mol. Biol. 51 (1980) 211-253. [PMID: 6255773]