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Literature summary extracted from

  • Leskovac, V.; Trivic, S.; Pericin, D.
    The three zinc-containing alcohol dehydrogenases from bakers' yeast, Saccharomyces cerevisiae (2002), FEMS Yeast Res., 2, 481-494.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.1 isozyme YADH-1, crystal structure analysis Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.1 D223G highly reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 D223G/G225R nearly inactive mutant Saccharomyces cerevisiae
1.1.1.1 D49N highly reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 DELTAA200/A201L highly reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 E68Q highly reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 G204A nearly inactive mutant Saccharomyces cerevisiae
1.1.1.1 G224I reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 G225R reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 H47R reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 H51E highly reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 H51Q reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 L203A reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 L203A/T178S reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 M294L increased activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 S198F highly reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 S269I nearly inactive mutant Saccharomyces cerevisiae
1.1.1.1 T48A inactive mutant Saccharomyces cerevisiae
1.1.1.1 T48C inactive mutant Saccharomyces cerevisiae
1.1.1.1 T48S reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 T48S/T93A reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 T48S/W57M/W93A reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 W57L reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 W57M slightly reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.1 W93A reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.1 additional information
-
 additional information wild-type and mutant forms of the 3 isozymes, steady-state kinetics, detailed kinetic analysis, at different pH values and temperatures Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.1 Zn2+ all isozymes, amino acid residues involved in zinc in binding are Cys46, Cys174, His67, Glu68, Asp49, and Thr48, binding mode Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Saccharomyces cerevisiae
-
 isozyme YADH-1, YADH-2, and YADH-3
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.1 a primary alcohol + NAD+ = an aldehyde + NADH + H+ detailed determination of the reaction and kinetic mechanisms, active site structure and determination of amino acid residues involved in catalysis, 3 isozymes Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 (S)-2-butanol + NAD+
-
 Saccharomyces cerevisiae 2-butanone + NADH
-
 r
1.1.1.1 allyl alcohol + NAD+
-
 Saccharomyces cerevisiae acrolein + NADH
-
 r
1.1.1.1 ethanol + NAD+
-
 Saccharomyces cerevisiae acetaldehyde + NADH
-
 r
1.1.1.1 ethylenglycol + NAD+
-
 Saccharomyces cerevisiae ? + NADH
-
 r
1.1.1.1 additional information substrate specificity and stereospecificity, substrate binding pocket structure of the 3 isozymes, involving Met294, Trp57, and Trp93 Saccharomyces cerevisiae ?
-
 ?
1.1.1.1 n-butanol + NAD+
-
 Saccharomyces cerevisiae n-butanal + NADH
-
 r
1.1.1.1 n-decanol + NAD+
-
 Saccharomyces cerevisiae n-decanal + NADH
-
 r
1.1.1.1 n-hexanol + NAD+
-
 Saccharomyces cerevisiae n-hexanal + NADH
-
 r
1.1.1.1 n-propanol + NAD+
-
 Saccharomyces cerevisiae n-propanal + NADH
-
 r
1.1.1.1 Tris + NAD+
-
 Saccharomyces cerevisiae ? + NADH
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.1 YADH
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.1 25 30 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 NAD+ cofactor binding mode Saccharomyces cerevisiae
1.1.1.1 NADH cofactor binding mode Saccharomyces cerevisiae