Bivalent cations stabilize yeast alcohol dehydrogenase I

Détails

ID Serval
serval:BIB_9B35F6E888B8
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Bivalent cations stabilize yeast alcohol dehydrogenase I
Périodique
Biochemical Journal
Auteur⸱e⸱s
De Bolle  X., Vinals  C., Fastrez  J., Feytmans  E.
ISSN
0264-6021 (Print)
Statut éditorial
Publié
Date de publication
04/1997
Volume
323
Numéro
2
Pages
409-413
Notes
Journal Article --- Old month value: Apr 15
Résumé
The thermostability of yeast alcohol dehydrogenase (ADH) I is strongly dependent on the presence of NaCl, a salt that is almost neutral on the Hofmeister scale, which suggests that solvent-accessible electrostatic repulsion might play a role in the inactivation of the enzyme. Moreover, CaCl2 and MgCl2 are able to stabilize the enzyme at millimolar concentrations. Ca2+ stabilizes yeast ADH I by preventing the dissociation of the reduced form of the enzyme and by preventing the unfolding of the oxidized form of the enzyme. An analysis of several chimaeric ADHs suggests that Ca2+ is fixed by the Asp-236 and Glu-101 side chains in yeast ADH I, but that Ca2+ can be displaced by replacing Met-168 by an Arg residue, as suggested by a three-dimensional model of the enzyme structure. These results indicate that electrostatic repulsion can cause protein unfolding and/or dissociation. It is proposed that yeast ADH I binds Mg2+ in vivo.
Mots-clé
Alcohol Dehydrogenase/chemistry/*metabolism Amino Acids/analysis Calcium Chloride/pharmacology Cations, Divalent/*pharmacology Enzyme Stability Heat Kinetics Magnesium Chloride/pharmacology Protein Conformation Saccharomyces cerevisiae Sodium Chloride/pharmacology
Pubmed
Web of science
Création de la notice
28/01/2008 11:03
Dernière modification de la notice
20/08/2019 15:02
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