Backbone assignment of double labelled 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe

Citation

Uhrinova S, Uhrin D, Nairn J, Price NC, Fothergill-Gilmore LA & Barlow PN (1997) Backbone assignment of double labelled 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe. Journal of Biomolecular NMR, 10 (3), pp. 309-310. https://doi.org/10.1023/A%3A1018307210607

Abstract
First paragraph: Phosphoglycerate mutase (PGAM) is the glycolytic enzyme that catalyses the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in the glycolytic pathway. In humans the functional enzyme exists as a homodimer of either 29-kDa or 30-kDa subunits (M-type or Etype respectively) whilst in yeasts it is found either as a tetramer (Saccharomyces cerevisiae), or as a monomer (Schizosaccharomyces pombe) (Nairn et al., 1994,1996). The PGAM from S. pombe (211 residues, 23.7 kDa), like the human PGAM, is dependent upon 2,3-bisphosphoglycerate (BPG) for activity. No crystal structure exists for the monomeric PGAM, nor for any PGAM in complex with its substrates or inhibitors. Therefore, highresolution NMR studies of S. pombe PGAM will provide valuable insights into subunit interactions within oligomeric PGAMs, the binding of substrates and inhibitors, and the mode of catalysis.

Keywords
phosphoglycerate mutase; backbone assignment; triple resonance NMR

Journal
Journal of Biomolecular NMR: Volume 10, Issue 3