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Literature summary for 1.1.1.71 extracted from

  • Zheng, T.; Olson, D.G.; Tian, L.; Bomble, Y.J.; Himmel, M.E.; Lo, J.; Hon, S.; Shaw, A.J.; van Dijken, J.P.; Lynd, L.R.
    Cofactor specificity of the bifunctional alcohol and aldehyde dehydrogenase (AdhE) in wild-type and mutant Clostridium thermocellum and Thermoanaerobacterium saccharolyticum (2015), J. Bacteriol., 197, 2610-2619.
    View publication on PubMedView publication on EuropePMC
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.075
-
 NADPH moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus
0.088
-
 NADH wild-type, pH 7.0, 55°C Acetivibrio thermocellus
0.17
-
 NADH moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus
1.4
-
 acetaldehyde cosubstrate NADH, moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus
1.4
-
 acetaldehyde cosubstrate NADPH, moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus
1.6
-
 acetaldehyde wild-type, pH 7.0, 55°C Acetivibrio thermocellus

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus A0A0H3W5U9 bifunctional enzyme, C-terminal section belongs to the iron-containing alcohol dehydrogenase family, N-terminal section belongs to the aldehyde dehydrogenase family
-
Thermoanaerobacterium saccharolyticum A0A0H3W5V0 bifunctional enzyme, C-terminal section belongs to the iron-containing alcohol dehydrogenase family, N-terminal section belongs to the aldehyde dehydrogenase family
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + NADH + H+
-
 Acetivibrio thermocellus ethanol + NAD+
-
 ?
acetaldehyde + NADH + H+
-
 Thermoanaerobacterium saccharolyticum ethanol + NAD+
-
 ?
acetaldehyde + NADPH + H+
-
 Acetivibrio thermocellus ethanol + NADP+
-
 ?
acetaldehyde + NADPH + H+
-
 Thermoanaerobacterium saccharolyticum ethanol + NADP+
-
 ?
additional information in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. In high-ethanol-producing (ethanologen) strains of Thermoanaerobacterium saccharolyticum, both ALDH and ADH activities show increased NADPH-linked activity Thermoanaerobacterium saccharolyticum ?
-
 ?
additional information in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. The AdhE protein of the ethanologenic strain of Clostridium thermocellum has acquired high NADPH-linked ADH activity while maintaining NADH-linked ALDH and ADH activities at wild-type levels Acetivibrio thermocellus ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
210
-
 acetaldehyde cosubstrate NADPH, moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus
220
-
 acetaldehyde cosubstrate NADH, moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus
220
-
 NADH moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus
240
-
 NADH wild-type, pH 7.0, 55°C Acetivibrio thermocellus
240
-
 acetaldehyde wild-type, pH 7.0, 55°C Acetivibrio thermocellus
280
-
 NADPH moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus

Cofactor

Cofactor Comment Organism Structure
NADH in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. In high-ethanol-producing (ethanologen) strains of Thermoanaerobacterium saccharolyticum, both ALDH and ADH activities show increased NADPH-linked activity Thermoanaerobacterium saccharolyticum
NADH in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. The AdhE protein of the ethanologenic strain of Clostridium thermocellum has acquired high NADPH-linked ADH activity while maintaining NADH-linked ALDH and ADH activities at wild-type levels Acetivibrio thermocellus
NADPH in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. In high-ethanol-producing (ethanologen) strains of Thermoanaerobacterium saccharolyticum, both ALDH and ADH activities show increased NADPH-linked activity Thermoanaerobacterium saccharolyticum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
150
-
 acetaldehyde cosubstrate NADH, moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus
150
-
 acetaldehyde cosubstrate NADPH, moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus
150
-
 acetaldehyde wild-type, pH 7.0, 55°C Acetivibrio thermocellus
1300
-
 NADH moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus
2700
-
 NADH wild-type, pH 7.0, 55°C Acetivibrio thermocellus
3700
-
 NADPH moderately ethanol producing strain, pH 7.0, 55°C Acetivibrio thermocellus