Bivalent cations stabilize yeast alcohol dehydrogenase I

Details

Serval ID
serval:BIB_9B35F6E888B8
Type
Article: article from journal or magazin.
Collection
Publications
Title
Bivalent cations stabilize yeast alcohol dehydrogenase I
Journal
Biochemical Journal
Author(s)
De Bolle  X., Vinals  C., Fastrez  J., Feytmans  E.
ISSN
0264-6021 (Print)
Publication state
Published
Issued date
04/1997
Volume
323
Number
2
Pages
409-413
Notes
Journal Article --- Old month value: Apr 15
Abstract
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.
Keywords
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
Create date
28/01/2008 11:03
Last modification date
20/08/2019 15:02
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