The amino acid sequence of yeast phosphoglycerate mutase

Abstract

The complete amino acid sequence of yeast phosphoglycerate mutase comprising 241 residues has been determined. The sequence was deduced from the two cyanogen bromide fragments, and from the peptides derived from these fragments after digestion by a number of proteolytic enzymes. Determination of this sequence now allows a detailed interpretation of the existing high-resolution X-ray crystallographic structure. A comparison of the sequence reported here with the sequences of peptides from phosphoglycerate mutases from other species, and with the sequence of erythrocyte diphosphoglycerate mutase, indicates that these enzymes have a high degree of structural homology. Autolysis of phosphoglycerate mutase by yeast extracts leads to the complete loss of mutase activity, and the formation of electrophoretically distinguishable forms (R. Sasaki, E. Sugimoto & H. Chiba, Archs Biochem. Biophys. 115, 53-61 (1966)). It is apparent from the amino acid sequence that these changes are due to the loss of an 8─12 residue peptide from the C-terminus.

Denaturation and renaturation of the monomeric phosphoglycerate mutase from Schizosaccharomyces pombe

“…pombe enzyme can be estimated as 5.6; this number is similar to that found (5) in the subunits of the enzymes from baker's yeast (Fothergill & Harkins, 1982) and rabbit muscle (Johnson & Price, 1987). The average degree of exposure of the tryptophan side chains in the S. pombe enzyme was assessed by the relative fluorescence quenching caused by succinimide and acrylamide (Eftink & Ghiron, 1984).…”

Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.

“…The 470-amino acid sequence of mature 6-PF-2-K/Fru-2,6-P2ase from rat liver revealed a fragmentary similarity of the chain encircling His-258 (7) with that surrounding the activesite His-8 of yeast phosphoglycerate mutase (PGM) (8). His-8 in yeast PGM is transiently phosphorylated during catalysis (9).…”

Inactivation of rabbit muscle phosphoglycerate mutase by limited proteolysis with thermolysin

“…subunit Mr 27000, has been well characterized in terms of amino acid sequence (Fothergill & Harkins, 1982) and three-dimensional structure (Winn et al, 1981). The enzyme from rabbit muscle is a dimer of subunit Mr 28000 (Ray & Peck, 1972).…”

“…Both enzymes depend on the presence of the cofactor 2,3-bisphosphoglycerate for activity. Apart from the homology of a peptide around the histidine residue that becomes phosphorylated during the reaction mechanism (Haggarty & Fothergill, 1980;Fothergill & Harkins, 1982), little comparative structural information on the two enzymes is available.…”