| EC |
5.4.2.4 |
| Accepted name: |
bisphosphoglycerate mutase |
| 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 reaction of EC 5.4.2.11 [phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)] and EC 5.4.2.12 [phosphoglycerate mutase (2,3-diphosphoglycerate-independent)]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37211-69-1 |
| References: |
| 1. |
Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, 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] |
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| [EC 5.4.2.4 created 1961 as EC 2.7.5.4, transferred 1984 to EC 5.4.2.4] |
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