The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase

EMBO J. 1983;2(7):1213-20.

Abstract

The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase, comprising 239 residues, was determined. The sequence was deduced from the four cyanogen bromide fragments, and from the peptides derived from these fragments after digestion with a number of proteolytic enzymes. Comparison of this sequence with that of the yeast glycolytic enzyme, phosphoglycerate mutase, shows that these enzymes are 47% identical. Most, but not all, of the residues implicated as being important for the activity of the glycolytic mutase are conserved in the erythrocyte diphosphoglycerate mutase.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Biological Evolution
  • Bisphosphoglycerate Mutase / blood*
  • Cyanogen Bromide
  • Erythrocytes / enzymology*
  • Humans
  • Peptide Fragments / isolation & purification
  • Phosphoglycerate Mutase
  • Phosphotransferases / blood*
  • Saccharomyces cerevisiae / enzymology

Substances

  • Peptide Fragments
  • Phosphotransferases
  • Phosphoglycerate Mutase
  • Bisphosphoglycerate Mutase
  • Cyanogen Bromide