EC 5.4.2.4 - Bisphosphoglycerate mutase

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IntEnz Enzyme Nomenclature
EC 5.4.2.4

Names

Accepted name:
bisphosphoglycerate mutase
Other names:
2,3-bisphosphoglycerate mutase
2,3-diphosphoglycerate mutase
2,3-diphosphoglycerate synthase
2,3-diphosphoglyceromutase
BPGM
DPGM
biphosphoglycerate synthase
bisphosphoglycerate synthase
bisphosphoglyceromutase
diphosphoglycerate mutase
diphosphoglyceric mutase
diphosphoglyceromutase
glycerate phosphomutase
phosphoglyceromutase
2,3-bisphosphoglycerate synthase
Systematic name:
3-phospho-D-glycerate 1,2-phosphomutase

Reaction

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 reaction of EC 5.4.2.12 [phosphoglycerate mutase (2,3-diphosphoglycerate-independent)]. Formerly EC 2.7.5.4.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00158
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004082
CAS Registry Number: 37211-69-1
UniProtKB/Swiss-Prot: (18) [show] [UniProt]

References

  1. Ray, W.J., Jr. and Peck, E.J., Jr.
    Phosphomutases.
    In: Boyer, P.D. (Ed.) The Enzymes, 3rd ed. vol. 6, Academic Press, New York, 1972, 407-477
  2. Rose, Z.B.
    The purification and properties of diphosphoglycerate mutase from human erythrocytes.
    J. Biol. Chem. 243: 4810-4820 (1968). [PMID: 5687724]
  3. Rose Z.B.
    The enzymology of 2,3-bisphosphoglycerate.
    Adv. Enzymol. Relat. Areas Mol. Biol. 51: 211-253 (1980). [PMID: 6255773]

[EC 5.4.2.4 created 1961 as EC 2.7.5.4, transferred 1984 to EC 5.4.2.4]