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. 1983;2(7):1213–1220. doi: 10.1002/j.1460-2075.1983.tb01569.x

The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase.

N W Haggarty, B Dunbar, L A Fothergill
PMCID: PMC555258  PMID: 6313356

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.

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Selected References

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  1. Benesch R., Benesch R. E., Yu C. I. Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Proc Natl Acad Sci U S A. 1968 Feb;59(2):526–532. doi: 10.1073/pnas.59.2.526. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chanutin A., Curnish R. R. Effect of organic and inorganic phosphates on the oxygen equilibrium of human erythrocytes. Arch Biochem Biophys. 1967 Jul;121(1):96–102. doi: 10.1016/0003-9861(67)90013-6. [DOI] [PubMed] [Google Scholar]
  3. Chiba H., Sasaki R. Functions, of 2,3-bisphosphoglycerate and its metabolism. Curr Top Cell Regul. 1978;14:75–116. doi: 10.1016/b978-0-12-152814-0.50007-1. [DOI] [PubMed] [Google Scholar]
  4. Fothergill L. A., Fothergill J. E. Structural comparison of ovalbumins from nine different species. Eur J Biochem. 1970 Dec;17(3):529–532. doi: 10.1111/j.1432-1033.1970.tb01196.x. [DOI] [PubMed] [Google Scholar]
  5. HEILMANN J., BARROLLIER J., WATZKE E. Beitrag zur Aminosäurebestimmung auf Papierchromatogrammen. Hoppe Seylers Z Physiol Chem. 1957;309(4-6):219–220. [PubMed] [Google Scholar]
  6. Haggarty N. W., Fothergill L. A. Amino acid sequence of an active site fragment from human diphosphoglycerate mutase. FEBS Lett. 1980 May 19;114(1):124–126. doi: 10.1016/0014-5793(80)80874-x. [DOI] [PubMed] [Google Scholar]
  7. Han C. H., Rose Z. B. Active site phosphohistidine peptides from red cell bisphosphoglycerate synthase and yeast phosphoglycerate mutase. J Biol Chem. 1979 Sep 25;254(18):8836–8840. [PubMed] [Google Scholar]
  8. Hass L. F., Sheibley R. H., Kappel W. K., Miller K. B. A comparison of some of the physical and chemical properties of the phosphoglycerate mutases from human erythrocytes. Biochem Biophys Res Commun. 1976 Oct 4;72(3):976–983. doi: 10.1016/s0006-291x(76)80227-6. [DOI] [PubMed] [Google Scholar]
  9. Kappel W. K., Hass L. F. The isolation and partial characterization of diphosphoglycerate mutase from human erythrocytes. Biochemistry. 1976 Jan 27;15(2):290–295. doi: 10.1021/bi00647a008. [DOI] [PubMed] [Google Scholar]
  10. Mahoney W. C., Hermodson M. A. High-yield cleavage of tryptophanyl peptide bonds by o-iodosobenzoic acid. Biochemistry. 1979 Aug 21;18(17):3810–3814. doi: 10.1021/bi00584a026. [DOI] [PubMed] [Google Scholar]
  11. Offord R. E. Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups. Nature. 1966 Aug 6;211(5049):591–593. doi: 10.1038/211591a0. [DOI] [PubMed] [Google Scholar]
  12. Penke B., Ferenczi R., Kovács K. A new acid hydrolysis method for determining tryptophan in peptides and proteins. Anal Biochem. 1974 Jul;60(1):45–50. doi: 10.1016/0003-2697(74)90129-8. [DOI] [PubMed] [Google Scholar]
  13. Perkins R. E., Conroy S. C., Dunbar B., Fothergill L. A., Tuite M. F., Dobson M. J., Kingsman S. M., Kingsman A. J. The complete amino acid sequence of yeast phosphoglycerate kinase. Biochem J. 1983 Apr 1;211(1):199–218. doi: 10.1042/bj2110199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. RODWELL V. W., TOWNE J. C., GRISOLIA S. The kinetic properties of yeast and muscle phosphoglyceric acid mutase. J Biol Chem. 1957 Oct;228(2):875–890. [PubMed] [Google Scholar]
  15. Rose A. B., Dube S. The purification and kinetic properties of biophosphoglycerate synthase from horse red blood cells. Arch Biochem Biophys. 1976 Nov;177(1):284–292. doi: 10.1016/0003-9861(76)90438-0. [DOI] [PubMed] [Google Scholar]
  16. Rose Z. B. Evidence for a phosphohistidine protein intermediate in the phosphoglycerate mutase reaction. Arch Biochem Biophys. 1970 Oct;140(2):508–513. doi: 10.1016/0003-9861(70)90095-0. [DOI] [PubMed] [Google Scholar]
  17. Rose Z. B., Liebowitz J. 2,3-diphosphoglycerate phosphatase from human erythrocytes. General properties and activation by anions. J Biol Chem. 1970 Jun;245(12):3232–3241. [PubMed] [Google Scholar]
  18. Rose Z. B. The enzymology of 2,3-bisphosphoglycerate. Adv Enzymol Relat Areas Mol Biol. 1980;51:211–253. doi: 10.1002/9780470122969.ch5. [DOI] [PubMed] [Google Scholar]
  19. Rose Z. B. The phosphorylation of yeast phosphoglycerate mutase. Arch Biochem Biophys. 1971 Sep;146(1):359–360. doi: 10.1016/s0003-9861(71)80076-0. [DOI] [PubMed] [Google Scholar]
  20. Rose Z. B., Whalen R. G. The phosphorylation of diphosphoglycerate mutase. J Biol Chem. 1973 Mar 10;248(5):1513–1519. [PubMed] [Google Scholar]
  21. Sasaki R., Hirose M., Sugimoto E., Chiba H. Studies on a role of the 2,3-diphosphoglycerate phosphatase activity in the yeast phosphoglycerate mutase reaction. Biochim Biophys Acta. 1971 Mar 10;227(3):595–607. doi: 10.1016/0005-2744(71)90010-6. [DOI] [PubMed] [Google Scholar]
  22. Sasaki R., Ikura K., Sugimoto E., Chiba H. Purification of bisphosphoglyceromutase, 2,3-bisphosphoglycerate phosphatase and phosphoglyceromutase from human erthrocytes. Three enzyme activities in one protein. Eur J Biochem. 1975 Jan 15;50(3):581–593. doi: 10.1111/j.1432-1033.1975.tb09899.x. [DOI] [PubMed] [Google Scholar]
  23. Sasaki R., Sugimoto R., Chiba H. Yeast phosphoglyceric acid mutase-modifying enzyme. Arch Biochem Biophys. 1966 Jul;115(1):53–61. doi: 10.1016/s0003-9861(66)81037-8. [DOI] [PubMed] [Google Scholar]
  24. Smith M. A., Gerrie L. M., Dunbar B., Fothergill J. E. Primary structure of bovine complement activation fragment C4a, the third anaphylatoxin. Purification and complete amino acid sequence. Biochem J. 1982 Nov 1;207(2):253–260. doi: 10.1042/bj2070253. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Winn S. I., Watson H. C., Fothergill L. A., Harkins R. N. The active site of yeast phosphoglycerate mutase. Biochem Soc Trans. 1977;5(3):657–659. doi: 10.1042/bst0050657. [DOI] [PubMed] [Google Scholar]
  26. Winn S. I., Watson H. C., Harkins R. N., Fothergill L. A. Structure and activity of phosphoglycerate mutase. Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26;293(1063):121–130. doi: 10.1098/rstb.1981.0066. [DOI] [PubMed] [Google Scholar]

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