The amino acid sequence of yeast phosphoglycerate mutase

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Abstract
The complete amino acid sequence of yeast phosphoglycerate mutase comprising 241 residues was determined. The sequence was deduced from the 2 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 (Sasaki et.al. 1966). It is apparent from the amino acid sequence that these changes are due to the loss the an 8-12 residue peptide from the carboxyl-terminus.