EC 5.4.2.12 - Phosphoglycerate mutase (2,3-diphosphoglycerate-independent)

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IntEnz Enzyme Nomenclature
EC 5.4.2.12

Names

Accepted name:
phosphoglycerate mutase (2,3-diphosphoglycerate-independent)
Other names:
cofactor independent phosphoglycerate mutase
2,3-diphosphoglycerate-independent phosphoglycerate mutase
phosphoglycerate phosphomutase [ambiguous]
phosphoglyceromutase [ambiguous]
monophosphoglycerate mutase [ambiguous]
monophosphoglyceromutase [ambiguous]
GriP mutase [ambiguous]
PGA mutase [ambiguous]
iPGM
iPGAM
PGAM-i
Systematic name:
D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-independent)

Reaction

Cofactor

Comments:

The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction.

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
UniProtKB/Swiss-Prot: (340) [show] [UniProt]

References

  1. Jedrzejas, M. J., Chander, M., Setlow, P., Krishnasamy, G.
    Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate.
    J. Biol. Chem. 275: 23146-23153 (2000). [PMID: 10764795]
  2. Rigden, D. J., Lamani, E., Mello, L. V., Littlejohn, J. E., Jedrzejas, M. J.
    Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling.
    J. Mol. Biol. 328: 909-920 (2003). [PMID: 12729763]
  3. Zhang, Y., Foster, J. M., Kumar, S., Fougere, M., Carlow, C. K.
    Cofactor-independent phosphoglycerate mutase has an essential role in Caenorhabditis elegans and is conserved in parasitic nematodes.
    J. Biol. Chem. 279: 37185-37190 (2004). [PMID: 15234973]
  4. Nukui, M., Mello, L. V., Littlejohn, J. E., Setlow, B., Setlow, P., Kim, K., Leighton, T., Jedrzejas, M. J.
    Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species.
    Biophys. J. 92: 977-988 (2007). [PMID: 17085493]
  5. Nowicki, M. W., Kuaprasert, B., McNae, I. W., Morgan, H. P., Harding, M. M., Michels, P. A., Fothergill-Gilmore, L. A., Walkinshaw, M. D.
    Crystal structures of Leishmania mexicana phosphoglycerate mutase suggest a one-metal mechanism and a new enzyme subclass.
    J. Mol. Biol. 394: 535-543 (2009). [PMID: 19781556]
  6. Mercaldi, G. F., Pereira, H. M., Cordeiro, A. T., Michels, P. A., Thiemann, O. H.
    Structural role of the active-site metal in the conformation of Trypanosoma brucei phosphoglycerate mutase.
    FEBS J. 279: 2012-2021 (2012). [PMID: 22458781]

[EC 5.4.2.12 created 2013]