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Literature summary extracted from

  • Vanni, A.; Anfossi, L.; Pessione, E.; Giovannoli, C.
    Catalytic and spectroscopic characterisation of a copper-substituted alcohol dehydrogenase from yeast (2002), Int. J. Biol. Macromol., 30, 41-45.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.1 12
-
 ethanol pH 7.5, 25°C, Co-ADH Saccharomyces cerevisiae
1.1.1.1 39
-
 ethanol pH 7.5, 25°C, Cu-ADH Saccharomyces cerevisiae
1.1.1.1 53
-
 ethanol pH 7.5, 25°C, native Zn-ADH Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.1 Co2+ construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview Saccharomyces cerevisiae
1.1.1.1 Cu2+ construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview Saccharomyces cerevisiae
1.1.1.1 Zn2+ native enzyme contains catalytic zinc ions Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.1 ethanol + NAD+ Saccharomyces cerevisiae rate-limiting step of the alcoholic fermentation acetaldehyde + NADH
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Saccharomyces cerevisiae
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.1.1.1 Zn2+ withdrawal by inactivation with Chelex 100, reactivation of the apoenzyme by addition of CuSO4, 1 h at 25°C, pH 7.6 Saccharomyces cerevisiae

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.1 commercial preparation lyophilized Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 2-propanol + NAD+
-
 Saccharomyces cerevisiae acetone + NADH
-
 ?
1.1.1.1 ethanol + NAD+
-
 Saccharomyces cerevisiae acetaldehyde + NADH
-
 ?
1.1.1.1 ethanol + NAD+ rate-limiting step of the alcoholic fermentation Saccharomyces cerevisiae acetaldehyde + NADH
-
 ?
1.1.1.1 n-butanol + NAD+
-
 Saccharomyces cerevisiae butyraldehyde + NADH
-
 ?
1.1.1.1 n-propanol + NAD+
-
 Saccharomyces cerevisiae propanal + NADH
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.1 Y-ADH
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.1 35
-
 Zn-ADH and Co-ADH Saccharomyces cerevisiae
1.1.1.1 40
-
 Cu-ADH Saccharomyces cerevisiae

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.1 15 50
-
 Saccharomyces cerevisiae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.1 56
-
 native Zn-ADH enzyme Saccharomyces cerevisiae
1.1.1.1 69
-
 Cu-ADH enzyme Saccharomyces cerevisiae
1.1.1.1 70
-
 above, Co-ADH enzyme Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.1 7.5
-
 Zn-ADH, Co-ADH, and Cu-ADH Saccharomyces cerevisiae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.1 6 9
-
 Saccharomyces cerevisiae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.1 6.5 9 native Zn-ADH enzyme Saccharomyces cerevisiae
1.1.1.1 6.5
-
 below, Cu-ADH and Co-ADH Saccharomyces cerevisiae