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. 1993 Apr 15;291(Pt 2):479–483. doi: 10.1042/bj2910479

Substitution of His-181 by alanine in yeast phosphoglycerate mutase leads to cofactor-induced dissociation of the tetrameric structure.

M F White 1, L A Fothergill-Gilmore 1, S M Kelly 1, N C Price 1
PMCID: PMC1132550  PMID: 8484729

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The structure and stability of a mutated yeast phosphoglycerate mutase in which His-181 has been replaced by alanine have been studied.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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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