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Literature summary extracted from

  • Wills, C.; Kratofil, P.; Londo, D.; Martin, T.
    Characterization of the two alcohol dehydrogenases of Zymomonas mobilis (1981), Arch. Biochem. Biophys., 210, 775-785.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.1.1.1 enzyme form ADH I is more stable during purification than enzyme form ADH-II Zymomonas mobilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.1 Zinc enzyme form ADH I and ADH II contain one zinc atom per subunit Zymomonas mobilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.1 31100
-
 2 * 31100, enzyme form ADH-II, SDS-PAGE Zymomonas mobilis
1.1.1.1 34700
-
 2 * 34700, enzyme form ADH-I, SDS-PAGE Zymomonas mobilis
1.1.1.1 67000
-
 enzyme form ADH-II, glycerol density gradient centrifugation Zymomonas mobilis
1.1.1.1 145000
-
 enzyme form ADH-I, glycerol density gradient centrifugation Zymomonas mobilis

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Zymomonas mobilis
-
 enzyme form ADH-I and ADH-II
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.1
-
 Zymomonas mobilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 allyl alcohol + NAD+
-
 Zymomonas mobilis prop-2-en-1-al + NADH
-
 ?
1.1.1.1 butanol + NAD+ oxidized by enzyme form ADH-I, no activity with enzyme form ADH-II Zymomonas mobilis butyraldehyde + NADH
-
 ?
1.1.1.1 ethanol + NAD+
-
 Zymomonas mobilis acetaldehyde + NADH
-
 ?
1.1.1.1 methanol + NAD+ no activity Zymomonas mobilis formaldehyde + NADH + H+
-
 ?
1.1.1.1 propan-2-ol + NAD+ very low activity Zymomonas mobilis acetone + NADH
-
 ?
1.1.1.1 propanol + NAD+
-
 Zymomonas mobilis propionaldehyde + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.1 dimer 2 * 34700, enzyme form ADH-I, SDS-PAGE Zymomonas mobilis
1.1.1.1 dimer 2 * 31100, enzyme form ADH-II, SDS-PAGE Zymomonas mobilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.1 9.5
-
 enzyme form ADH-I, oxidation of ethanol Zymomonas mobilis
1.1.1.1 10
-
 enzyme form ADH-II, oxidation of ethanol Zymomonas mobilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 NAD+
-
 Zymomonas mobilis
1.1.1.1 NADH
-
 Zymomonas mobilis