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Literature summary for 1.1.1.1 extracted from

  • Kinoshita, S.; Kakizono, T.; Kadota, K.; Das, K.; Taguchi, H.
    Purification of two alcohol dehydrogenases from Zymomonas mobilis and their properties (1985), Appl. Microbiol. Biotechnol., 22, 249-254.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline 0.2 mM, strong inhibition Zymomonas mobilis
PCMB
-
Zymomonas mobilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
NADH enzyme form ADH II Zymomonas mobilis
0.027
-
NADH enzyme form ADH I Zymomonas mobilis
0.073
-
NAD+ enzyme form ADH I Zymomonas mobilis
0.086
-
acetaldehyde enzyme form ADH I Zymomonas mobilis
0.11
-
NAD+ enzyme form ADH II Zymomonas mobilis
1.3
-
acetaldehyde enzyme form ADH II Zymomonas mobilis
4.8
-
ethanol enzyme form ADH I Zymomonas mobilis
27
-
ethanol enzyme form ADH II Zymomonas mobilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
2 * 38000, enzyme form ADHII, SDS-PAGE Zymomonas mobilis
40000
-
2 * 40000, enzyme form ADHI Zymomonas mobilis
80000
-
enzyme form ADHI, gel filtration Zymomonas mobilis
95000
-
enzyme form ADHII, gel filtration Zymomonas mobilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Zymomonas mobilis key enzyme in ethanol production ?
-
?

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis
-
ADH I and ADH II
-

Purification (Commentary)

Purification (Comment) Organism
-
Zymomonas mobilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
93
-
enzyme form ADHI Zymomonas mobilis
470
-
enzyme form ADHII Zymomonas mobilis

Storage Stability

Storage Stability Organism
4°C, most stable at pH 7.5 during storage for 2 days Zymomonas mobilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + NADH + H+
-
Zymomonas mobilis ethanol + NAD+
-
r
allyl alcohol + NAD+
-
Zymomonas mobilis prop-2-en-1-al + NADH
-
?
butanol + NAD+ activity with ADH I, no activity with ADH II Zymomonas mobilis butyraldehyde + NADH
-
?
butyraldehyde + NADH activity with enzyme form ADH I, no activity with enzyme form ADH II Zymomonas mobilis n-butanol + NAD+
-
r
ethanol + NAD+
-
Zymomonas mobilis acetaldehyde + NADH
-
r
formaldehyde + NADH + H+ activity with ADH I, no activity with ADH II Zymomonas mobilis methanol + NAD+
-
?
furfural + NADH + H+ activity with enzyme form ADH I, no activity with enzyme form ADH II Zymomonas mobilis furfuryl alcohol + NAD+
-
r
furfuryl alcohol + NAD+ activity with ADH I, no activity with ADH II Zymomonas mobilis furfural + NADH
-
r
hexanol + NAD+ activity with ADH I, no activity with ADH II Zymomonas mobilis n-hexanal + NADH
-
?
methanol + NAD+ no activity Zymomonas mobilis formaldehyde + NADH + H+
-
?
additional information key enzyme in ethanol production Zymomonas mobilis ?
-
?
n-pentylaldehyde + NADH + H+
-
Zymomonas mobilis n-pentanol + NAD+
-
r
octan-1-ol + NAD+ activity with ADH I, no activity with ADH II Zymomonas mobilis n-octanal + NADH
-
?
pentanol + NAD+ activity with ADH I, no activity with ADH II Zymomonas mobilis n-pentanal + NADH
-
?
propan-2-ol + NAD+
-
Zymomonas mobilis acetone + NADH
-
?
propanol + NAD+
-
Zymomonas mobilis propionaldehyde + NADH + H+
-
?
propionaldehyde + NADH
-
Zymomonas mobilis propanol + NAD+
-
?

Subunits

Subunits Comment Organism
dimer 2 * 38000, enzyme form ADHII, SDS-PAGE Zymomonas mobilis
dimer 2 * 40000, enzyme form ADHI Zymomonas mobilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
inactivation constant for ADHI: 1.23 per min, inactivation constant for ADH II: 0.13 per min Zymomonas mobilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
reduction of acetaldehyde, enzyme form ADH I Zymomonas mobilis
6.5
-
reduction of acetaldehyde, enzyme form ADH II Zymomonas mobilis
9.5
-
enzyme form ADH-I, oxidation of ethanol Zymomonas mobilis
10
-
enzyme form ADH-II, oxidation of ethanol Zymomonas mobilis

pH Stability

pH Stability pH Stability Maximum Comment Organism
7.5
-
4°C, stable for 2 days Zymomonas mobilis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Zymomonas mobilis
NADH
-
Zymomonas mobilis