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Literature summary for 1.1.1.144 extracted from

  • Hoellrigl, V.; Hollmann, F.; Kleeb, A.C.; Buehler, K.; Schmid, A.
    TADH, the thermostable alcohol dehydrogenase from Thermus sp. ATN1: a versatile new biocatalyst for organic synthesis (2008), Appl. Microbiol. Biotechnol., 81, 263-273.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Thermus sp.
-
-
-
Thermus sp. ATN1
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-perillylalcohol + NAD+ 52% activity compared to cyclohexanol Thermus sp. (S)-perillaldehyde + NADH + H+
-
?
(S)-perillylalcohol + NAD+ 52% activity compared to cyclohexanol Thermus sp. ATN1 (S)-perillaldehyde + NADH + H+
-
?

Synonyms

Synonyms Comment Organism
ADH
-
Thermus sp.

Cofactor

Cofactor Comment Organism Structure
NAD+ dependent on Thermus sp.