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Literature summary for 1.1.1.1 extracted from

  • Nagel, Z.D.; Cun, S.; Klinman, J.P.
    Identification of a long-range protein network that modulates active site dynamics in extremophilic alcohol dehydrogenases (2013), J. Biol. Chem., 288, 14087-14097.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Geobacillus stearothermophilus
expression in Escherichia coli Moraxella sp.

Protein Variants

Protein Variants Comment Organism
A25Y mutation in the dimer-dimer interface, leads to a more thermostable enzyme and a change in the rate-determining step at low temperature Moraxella sp.
W87A mutation results in a loss of the Arrhenius break seen at 30°C for the wild-type enzyme and an increase in cold lability due to destabilization of the active tetrameric form. Kinetic isotope effects are nearly temperature-independent over the experimental temperature range, and similar in magnitude to those measured above 30°C for the wild-type enzyme Geobacillus stearothermophilus
Y25A mutation in the dimer-dimer interface, results in kinetic behavior similar to that of mutantion W87A Geobacillus stearothermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 NAD+ mutant W87A, pH 7.0, 30°C Geobacillus stearothermophilus
0.5
-
 NAD+ mutant A25Y, pH 7.0, 30°C Moraxella sp.
1
-
 NAD+ mutant Y25A, pH 7.0, 30°C Geobacillus stearothermophilus
1.1
-
 NAD+ wild-type, pH 7.0, 30°C Geobacillus stearothermophilus
1.5
-
 benzyl alcohol mutant W87A, pH 7.0, 30°C Geobacillus stearothermophilus
6.9
-
 benzyl alcohol wild-type, pH 7.0, 30°C Geobacillus stearothermophilus
7.2
-
 benzyl alcohol mutant Y25A, pH 7.0, 30°C Geobacillus stearothermophilus
16
-
 benzyl alcohol mutant A25Y, pH 7.0, 30°C Moraxella sp.
29.4
-
 benzyl alcohol wild-type, pH 7.0, 30°C Moraxella sp.

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P42328
-
-
Moraxella sp. Q8GIX7
-
-
Moraxella sp. TAE123 Q8GIX7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyl alcohol + NAD+
-
 Geobacillus stearothermophilus benzaldehyde + NADH + H+
-
 ?
benzyl alcohol + NAD+
-
 Moraxella sp. benzaldehyde + NADH + H+
-
 ?
benzyl alcohol + NAD+
-
 Moraxella sp. TAE123 benzaldehyde + NADH + H+
-
 ?
additional information mutation at the substrate-binding site, or at a dimer interface, alters kinetic properties and protein oligomeric structure, active site flexibility is correlated with subunit interactions 20 A away Geobacillus stearothermophilus ?
-
 ?
additional information mutation at the substrate-binding site, or at a dimer interface, alters kinetic properties and protein oligomeric structure, active site flexibility is correlated with subunit interactions 20 A away Moraxella sp. ?
-
 ?
additional information mutation at the substrate-binding site, or at a dimer interface, alters kinetic properties and protein oligomeric structure, active site flexibility is correlated with subunit interactions 20 A away Moraxella sp. TAE123 ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.8
-
 benzyl alcohol mutant A25Y, pH 7.0, 30°C Moraxella sp.
5.5
-
 benzyl alcohol mutant W87A, pH 7.0, 30°C Geobacillus stearothermophilus
6.9
-
 benzyl alcohol wild-type, pH 7.0, 30°C Moraxella sp.
14
-
 benzyl alcohol mutant Y25A, pH 7.0, 30°C Geobacillus stearothermophilus
24.9
-
 benzyl alcohol wild-type, pH 7.0, 30°C Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Geobacillus stearothermophilus
NAD+
-
 Moraxella sp.