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Literature summary for 1.1.1.1 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)

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

Protein Variants

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

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

Organism

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

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
YADH
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

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

Cofactor

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