Substitution of HIS-181 by Alanine in yeast phosphoglycerate mutase leads to cofactor-induced dissociation of the tetrameric structure

Malcolm F White, L A Fothergillgilmore, S M Kelly, N C Price

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)

Abstract

The structure and stability of a mutated yeast phosphoglycerate mutase in which His-181 has been replaced by alanine have been studied. The secondary, tertiary and quaternary structures of the mutant enzyme in the absence of ligands are essentially identical to those of the wild-type enzyme as revealed by c.d., fluorescence and cross-linking studies. The mutant enzyme is slightly less stable than the wild-type enzyme towards denaturation by guanidium chloride (GdnHCl). On addition of cofactor 2,3-bisphosphoglycerate, the wild-type enzyme shows increased stability towards GdnHCl. However, addition of cofactor causes dramatic changes in the structure of the mutant enzyme, leading to dissociation of the tetrameric form to dimeric and monomeric species.

Original languageEnglish
Pages (from-to)479-483
Number of pages5
JournalBiochemical Journal
Volume291
Publication statusPublished - 15 Apr 1993

Keywords

  • RECONSTITUTION
  • DEHYDROGENASE

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