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Literature summary for 1.1.1.B3 extracted from

  • Protsko, C.; Vieille, C.; Laivenieks, M.; Prasad, L.; Sanders, D.A.; Delbaere, L.T.
    Crystallization and preliminary X-ray diffraction analysis of the Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase I86A mutant (2010), Acta Crystallogr. Sect. F, 66, 831-833.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
I86A site-directed mutagensis, the secondary alcohol dehydrogenase I86A mutant is stereospecific for (R)-alcohols instead of (S)-alcohols, in contrast to the wild-type enzyme, the mutation I86A allows large substituents to fit into the large pocket of I86ATeSADH, which corresponds to the small pocket in wild-type TeSADH, modeling of the stereopreference of TeSADH I86A Thermoanaerobacter ethanolicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-1-phenylethanol + NAD+ Thermoanaerobacter ethanolicus activity of the wild-type enzyme, the mutant I886A is (R)-specific forming (R)-1-phenylethanol acetophenone + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Thermoanaerobacter ethanolicus P77990 gene adhB
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-1-phenylethanol + NAD+ activity of the wild-type enzyme, the mutant I886A is (R)-specific forming (R)-1-phenylethanol Thermoanaerobacter ethanolicus acetophenone + NADH + H+
-
r

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Thermoanaerobacter ethanolicus
NADH
-
Thermoanaerobacter ethanolicus