Congratulations to Yunus Ensari and Gaurao V. Dhoke on their recent Publication!


Engineering of Candida parapsilosis alcohol dehydrogenase for conversion of methyl 3-hydroxyalkanoates

Engineering of a Candida parapsilosis alcohol dehydrogenase Copyright: Bio VI

Expanding the substrate scope of enzymes opens up new routes for the synthesis of valuable chemicals. Ketone-functionalized fatty acid derivatives and corresponding chiral alcohols are valuable building blocks for the synthesis of a variety of chemicals including pharmaceuticals.

Candida parapsilosis alcohol dehydrogenase wild type is an S-selective alcohol dehydrogenase that does not convert 3-hydroxy fatty acid methyl esters larger than methyl 3-hydroxypentanoate. Thus, methyl 3-hydroxyhexanoate and methyl (R)-3-hydroxybutyrate are not accepted as substrate by wild type Candida parapsilosis alcohol dehydrogenase. Enlarging the binding pocket of the wild type enzyme through substitution of tryptophan at position 286 by alanine led to a chain length specificity shift and oxidation of methyl 3-hydroxyhexanoate to the corresponding ketone. Furthermore, a second variant with double substitution on positions 119 and 286 exhibited inverted enantiopreference for methyl 3-hydroxybutyrate from the S-enantiomer to the R-enantiomer.

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Y. Ensari, G. V. Dhoke, M. D. Davari, M. Bocola, A. J. Ruff, U. Schwaneberg, Chem. Eur. J. 2017, 23, 12636.