EC - Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)

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IntEnz Enzyme Nomenclature


Accepted name:
phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)
Other names:
GriP mutase [ambiguous]
PGA mutase [ambiguous]
glycerate phosphomutase (diphosphoglycerate cofactor)
monophosphoglycerate mutase [ambiguous]
monophosphoglyceromutase [ambiguous]
phosphoglycerate phosphomutase [ambiguous]
phosphoglyceromutase [ambiguous]
2,3-diphosphoglycerate dependent phosphoglycerate mutase
cofactor dependent phosphoglycerate mutase
Systematic name:
D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-dependent)



The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC, phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC, bisphosphoglycerate mutase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00158
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (443) [show] [UniProt]


  1. Grisolia, S.
    Phosphoglyceric acid mutase.
    Methods Enzymol. 5 : 236-242 (1962).
  2. Ray, W.J., Jr. and Peck, E.J., Jr.
    In: Boyer, P.D. (Ed.) The Enzymes , 3rd ed. vol. 6 , Academic Press , New York , 1972 , 407-477
  3. Rose, Z.B.
    The enzymology of 2,3-bisphosphoglycerate.
    Adv. Enzymol. Relat. Areas Mol. Biol. 51 : 211-253 (1980). [PMID: 6255773]
  4. Rigden, D. J., Walter, R. A., Phillips, S. E., Fothergill-Gilmore, L. A.
    Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism.
    J. Mol. Biol. 286 : 1507-1517 (1999). [PMID: 10064712]
  5. Bond, C. S., White, M. F., Hunter, W. N.
    High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase.
    J. Biol. Chem. 276 : 3247-3253 (2001). [PMID: 11038361]
  6. Rigden, D. J., Mello, L. V., Setlow, P., Jedrzejas, M. J.
    Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity.
    J. Mol. Biol. 315 : 1129-1143 (2002). [PMID: 11827481]
  7. Rigden, D. J., Littlejohn, J. E., Henderson, K., Jedrzejas, M. J.
    Structures of phosphate and trivanadate complexes of Bacillus stearothermophilus phosphatase PhoE: structural and functional analysis in the cofactor-dependent phosphoglycerate mutase superfamily.
    J. Mol. Biol. 325 : 411-420 (2003). [PMID: 12498792]

[EC created 1961 as EC (EC created 1961, incorporated 1984) transferred 2013 to]