The Enzyme Database

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EC 5.4.2.12     
Accepted name: phosphoglycerate mutase (2,3-diphosphoglycerate-independent)
Reaction: 2-phospho-D-glycerate = 3-phospho-D-glycerate
For diagram of the Entner-Doudoroff pathway, click here
Other name(s): 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)
Comments: The enzymes from higher plants, algae, 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: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jedrzejas, M.J., Chander, M., Setlow, P. and 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 (2000) 23146–23153. [PMID: 10764795]
2.  Rigden, D.J., Lamani, E., Mello, L.V., Littlejohn, J.E. and 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 (2003) 909–920. [PMID: 12729763]
3.  Zhang, Y., Foster, J.M., Kumar, S., Fougere, M. and Carlow, C.K. Cofactor-independent phosphoglycerate mutase has an essential role in Caenorhabditis elegans and is conserved in parasitic nematodes. J. Biol. Chem. 279 (2004) 37185–37190. [PMID: 15234973]
4.  Nukui, M., Mello, L.V., Littlejohn, J.E., Setlow, B., Setlow, P., Kim, K., Leighton, T. and 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 (2007) 977–988. [PMID: 17085493]
5.  Nowicki, M.W., Kuaprasert, B., McNae, I.W., Morgan, H.P., Harding, M.M., Michels, P.A., Fothergill-Gilmore, L.A. and Walkinshaw, M.D. Crystal structures of Leishmania mexicana phosphoglycerate mutase suggest a one-metal mechanism and a new enzyme subclass. J. Mol. Biol. 394 (2009) 535–543. [PMID: 19781556]
6.  Mercaldi, G.F., Pereira, H.M., Cordeiro, A.T., Michels, P.A. and Thiemann, O.H. Structural role of the active-site metal in the conformation of Trypanosoma brucei phosphoglycerate mutase. FEBS J. 279 (2012) 2012–2021. [PMID: 22458781]
[EC 5.4.2.12 created 2013]
 
 


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