Enantioselective formation of carbon-nitrogen bonds is a reaction of great interest for the preparation of chiral intermediates. There are several classes of enzymes that catalyze such reactions, such as ammonia lyases, halohydrin dehalogenases, and aminotransferases. The ammonia lyases belong to different phylogenetic and mechanistic groups, including the MIO (4-methylidene-imidazole-5-one) dependent lyase/mutase superfamily of enzymes, which act on aromatic compounds, the aspartase/fumarase superfamily, which are active with aspartate, and the enolase superfamily enzymes, which includes lyases acting on substituted aspartic acids. Halohydrin dehalogenases can catalyze enantioselective carbon-nitrogen bond formation by ring opening of epoxides with N-nucleophiles, whereas aminotransferases convert ketones to amines. Although most of these enzymes have a rather narrow substrate range, some activity with synthetic substrates is often detectable. Protein engineering and directed evolution, inspired by mechanistic and structural insight, allows the generation of lyase variants with greatly enhanced biocatalytic performance.

Engineering promiscuous lyases for enantioselective biocatalysis

244th National Meeting (2012)

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