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Literature summary for 1.1.1.1 extracted from

  • De Bolle, X.; Vinals, C.; Fastrez, J.; Feytmans, E.
    Bivalent cations stabilize yeast alcohol dehydrogenase I (1997), Biochem. J., 323, 409-413.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
three-dimensional model of the enzyme structure suggest that Ca2+ can be displaced by replacing Met-168 by an Arg residue Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 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. Ca2+ is fixed by the Asp236 and Glu101 side chains in yeast ADH I Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Synonyms

Synonyms Comment Organism
ADH I
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Saccharomyces cerevisiae