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Literature summary for 1.1.1.21 extracted from

  • Zheng, T.; Olson, D.G.; Murphy, S.J.; Shao, X.; Tian, L.; Lynd, L.R.
    Both adhE and a separate NADPH-dependent alcohol dehydrogenase (adhA) are necessary for high ethanol production in Thermoanaerobacterium saccharolyticum (2017), J. Bacteriol., 199, e00542-16.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermoanaerobacterium saccharolyticum

Metals/Ions

Metals/Ions Comment Organism Structure
Iron
-
Thermoanaerobacterium saccharolyticum

Organism

Organism UniProt Comment Textmining
Thermoanaerobacterium saccharolyticum
-
-
-
Thermoanaerobacterium saccharolyticum LL1049
-
-
-

Purification (Commentary)

Purification (Comment) Organism
AdhA appears to be insensitive to the presence of oxygen Thermoanaerobacterium saccharolyticum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.8
-
pH 7.0, 55°C Thermoanaerobacterium saccharolyticum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + NADPH + H+
-
Thermoanaerobacterium saccharolyticum ethanol + NADP+
-
?
acetaldehyde + NADPH + H+
-
Thermoanaerobacterium saccharolyticum LL1049 ethanol + NADP+
-
?

Synonyms

Synonyms Comment Organism
AdhA
-
Thermoanaerobacterium saccharolyticum

Cofactor

Cofactor Comment Organism Structure
NADH about 4% of the activity with NADPH Thermoanaerobacterium saccharolyticum
NADPH
-
Thermoanaerobacterium saccharolyticum

General Information

General Information Comment Organism
physiological function gene deletion of adhA reduces ethanol production by about 50%, whereas multiple gene deletions of all annotated alcohol dehydrogenases except adhA and adhE does not affect ethanol production. Deletion of adhA in wild-type reduces NADPH-linked ADH activity (acetaldehyde-reducing) by 93% Thermoanaerobacterium saccharolyticum