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PMID: 6313356 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase.

The EMBO journal ·Vol. 2 ·No. 7 ·1983-00-00 ·Pages 1213-20

Haggarty NW, Dunbar B, Fothergill LA

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.

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
Chemicals
Peptide Fragments Phosphotransferases Phosphoglycerate Mutase Bisphosphoglycerate Mutase Cyanogen Bromide
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Haggarty N W
Dunbar B
Fothergill L A
References (26)
26 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1983-00-00
Pages
1213-20
Language
English
Region
England
NLM ID
8208664
PMCID
PMC555258
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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