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Exploring bacterial carboxylate reductases for the reduction of bifunctional carboxylic acids

19:31 EDT 1 Aug 2017 | Wiley Biotechnology Journal

Carboxylic acid reductases (CARs) selectively reduce carboxylic acids to aldehydes using ATP and NADPH as cofactors under mild conditions. Although CARs have attracted significant interest, only a few enzymes have been characterized to date, whereas the vast majority of CARs have yet to be examined. Herein we report that 12 bacterial CARs reduced a broad range of bifunctional carboxylic acids containing oxo‐, hydroxy‐, amino‐, or second carboxyl groups with several enzymes showing activity toward 4‐hydroxybutanoic (4‐HB) and adipic acids. These CARs exhibited significant reductase activity against substrates whose second functional group is separated from the carboxylate by at least three carbons with both carboxylate groups being reduced in dicarboxylic acids. Purified CARs supplemented with cofactor regenerating systems (for ATP and NADPH), an inorganic pyrophosphatase, and an aldo‐keto reductase catalyzed a high conversion (50‐76%) of 4‐HB to 1,4‐butanediol (1,4‐BDO) and adipic acid to 1,6‐hexanediol (1,6‐HDO). Likewise, Escherichia coli strains expressing eight different CARs efficiently reduced 4‐HB to 1,4‐BDO with 50‐95% conversion, whereas adipic acid was reduced to a mixture of 6‐hydroxyhexanoic acid (6‐HHA) and 1,6‐HDO. Thus, our results illustrate the broad biochemical diversity of bacterial CARs and their compatibility with other enzymes for applications in biocatalysis.

Original Article: Exploring bacterial carboxylate reductases for the reduction of bifunctional carboxylic acids

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