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Literature summary extracted from

  • Gillooly, D.J.; Fewson, C.A.
    Production of a perillyl alcohol dehydrogenase by site-directed mutagenesis of a benzyl alcohol dehydrogenase (1998), Biotechnol. Lett., 20, 325-327.
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.144 R50H mutation of active site arginine to a histidine can switch substrate specificity of the enzyme benzyl alcohol dehydrogenase (EC 1.1.1.90) so that it has a very much greater preference for perillyl alcohol than for benzyl alcohol Acinetobacter calcoaceticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.144 0.119
-
 perillyl alcohol mutant benzyl alcohol dehydrogenase Acinetobacter calcoaceticus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.144 Acinetobacter calcoaceticus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.144 perillyl alcohol + NAD+
-
 Acinetobacter calcoaceticus perillyl aldehyde + NADH
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.144 84
-
 perillyl alcohol mutant benzyl alcohol dehydrogenase Acinetobacter calcoaceticus