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Literature summary for 1.1.1.71 extracted from

  • Timpson, L.M.; Alsafadi, D.; Mac Donnchadha, C.; Liddell, S.; Sharkey, M.A.; Paradisi, F.
    Characterization of alcohol dehydrogenase (ADH12) from Haloarcula marismortui, an extreme halophile from the Dead Sea (2012), Extremophiles, 16, 57-66.
    View publication on PubMed
Search for more literature for 1.1.1.71

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli as a His-tagged protein Haloarcula marismortui

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.029
-
 NADPH pH 6.0, 50°C Haloarcula marismortui
0.101
-
 NADP+ pH 10.0, 50°C Haloarcula marismortui
5.1
-
 acetaldehyde pH 6.0, 50°C Haloarcula marismortui

Metals/Ions

Metals/Ions Comment Organism Structure
K+ optimally active in the presence of 2 M KCl Haloarcula marismortui

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41600
-
 x * 41600, His-tagged protein, SDS-PAGE, mass spectrometry Haloarcula marismortui

Organic Solvent Stability

Organic Solvent Comment Organism
acetonitrile 10%, enzyme retains 69% of activity following incubation Haloarcula marismortui
dimethyl sulfoxide 10%, enzyme retains 78% of activity following incubation Haloarcula marismortui
tetrahydrofuran 10%, decativates Haloarcula marismortui

Organism

Organism UniProt Comment Textmining
Haloarcula marismortui Q5V676
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloarcula marismortui

Storage Stability

Storage Stability Organism
-20°C, retains approximately 80% of its original activity after 10 days Haloarcula marismortui

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-butanol + NADP+ 117% of the activity compared to ethanol Haloarcula marismortui butanal + NADPH + H+
-
 ?
1-pentanol + NADP+ 74% of the activity compared to ethanol Haloarcula marismortui pentanal + NADPH + H+
-
 ?
1-propanol + NADP+ 137% of the activity compared to ethanol Haloarcula marismortui propanal + NADPH + H+
-
 ?
2-butanol + NADP+ 43% of the activity compared to ethanol Haloarcula marismortui 2-butanone + NADPH + H+
-
 ?
acetaldehyde + NADPH + H+
-
 Haloarcula marismortui ethanol + NADP+
-
 ?
ethanol + NAD+ enzyme appears to preferentially catalyze the reductive reaction. Activity with NAD+ is 75% less than that detected with NADP+ Haloarcula marismortui acetaldehyde + NADH + H+
-
 ?
ethanol + NADP+ enzyme appears to preferentially catalyze the reductive reaction. Activity with NAD+ is 75% less than that detected with NADP+ Haloarcula marismortui acetaldehyde + NADPH + H+
-
 ?
additional information the enzyme does not accept methanol, 2-propanol, glycerol or glucose as substrates Haloarcula marismortui ?
-
 ?

Subunits

Subunits Comment Organism
? x * 41600, His-tagged protein, SDS-PAGE, mass spectrometry Haloarcula marismortui

Synonyms

Synonyms Comment Organism
ADH12
-
 Haloarcula marismortui

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Haloarcula marismortui

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 80 40°C: about 50% of maximal activity, 80°C: about 70% of maximal activity Haloarcula marismortui

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 reductive reaction Haloarcula marismortui
10
-
 oxidative reaction Haloarcula marismortui

Cofactor

Cofactor Comment Organism Structure
NAD+ activity is 75% less than that detected with NADP+ Haloarcula marismortui
NADP+ preferred cofactor. Activity with NAD+ is 75% less than that detected with NADP+ Haloarcula marismortui