Reaction: 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
Other name(s): diphosphoglycerate mutase; glycerate phosphomutase; bisphosphoglycerate synthase; bisphosphoglyceromutase; biphosphoglycerate synthase; diphosphoglyceric mutase; 2,3-diphosphoglycerate mutase; phosphoglyceromutase; 2,3-diphosphoglycerate synthase; DPGM; 2,3-bisphosphoglycerate mutase; BPGM; diphosphoglyceromutase; 2,3-diphosphoglyceromutase
Systematic name: 3-phospho-D-glycerate 1,2-phosphomutase
Comments: In the direction shown, this enzyme is phosphorylated by 3-phosphoglyceroyl phosphate, to give phosphoenzyme and 3-phosphoglycerate. The latter is rephosphorylated by the enzyme to yield 2,3-bisphosphoglycerate, but this reaction is slowed by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. This enzyme also catalyses, slowly, the reactions of EC 184.108.40.206 (bisphosphoglycerate phosphatase), EC 220.127.116.11 [phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)] and EC 18.104.22.168 [phosphoglycerate mutase (2,3-diphosphoglycerate-independent)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37211-69-1
1. 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.
2. Rose, Z.B. The purification and properties of diphosphoglycerate mutase from human erythrocytes. J. Biol. Chem. 243 (1968) 4810-4820. [PMID: 5687724]
3. Rose, Z.B. The enzymology of 2,3-bisphosphoglycerate. Adv. Enzymol. Relat. Areas Mol. Biol. 51 (1980) 211-253. [PMID: 6255773]