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Literature summary for 1.1.1.1 extracted from

  • Ganzhorn, A.J.; Green, D.W.; Hershey, A.D.; Gould, R.M.; Plapp, B.V.
    Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity (1987), J. Biol. Chem., 262, 3754-3761.
    View publication on PubMed
Search for more literature for 1.1.1.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Saccharomyces cerevisiae
-
 Schizosaccharomyces pombe

Protein Variants

Protein Variants Comment Organism
M294L 7-10fold increase in reactivity, V/Km, with butanol, pentanol and hexanol Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
4-methoxypyrazole
-
 Saccharomyces cerevisiae
butyramide
-
 Saccharomyces cerevisiae
heptafluorobutanol
-
 Saccharomyces cerevisiae
trifluoroethanol
-
 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 isoenzyme I, II and III
-
Schizosaccharomyces pombe
-
-
-

Reaction

Reaction Comment Organism Reaction ID
a primary alcohol + NAD+ = an aldehyde + NADH + H+ mechanism is predominantly ordered with ethanol, but partially random with butanol Saccharomyces cerevisiae
a
a primary alcohol + NAD+ = an aldehyde + NADH + H+ mechanism is predominantly ordered with ethanol, but partially random with butanol Schizosaccharomyces pombe
a

Source Tissue

Source Tissue Comment Organism Textmining

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Saccharomyces cerevisiae
NAD+
-
 Schizosaccharomyces pombe
NADH
-
 Saccharomyces cerevisiae
NADH
-
 Schizosaccharomyces pombe