A series of synthetic nicotinamide cofactors were synthesized to replace natural nicotinamide cofactors and promote enoate reductase (ER)-catalyzed reactions without compromising activity or stereoselectivity of the bioreduction process. Conversions and enantioselectivities of up to >99% were obtained for C=C bioreductions and the process was successfully upscaled. Furthermore, high chemoselectivity was observed when employing these nicotinamide cofactor mimics (mNADs) with crude extracts in ER-catalyzed reactions.The asymmetric reduction of conjugated C=C double bonds using enoate reductases (ERs, EC 1.3.1.31) is receiving great interest in preparative organic chemistry.1 § Both authors contributed equally.

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During the last three decades the use of hydrolases for the catalysis of environmentally friendly organic processes under mild reaction conditions has been well documented. Hydrolases have shown themselves to be ideal tools for the acceleration of synthetic transformations because of their high stability, catalytic efficiency, commercial availability and broad substrate specificity in a wide spectrum of biocatalyzed processes. In recent years, novel examples have appeared related to non-conventional reactions catalyzed by hydrolytic enzymes. Amongst these, lipases and acylases have gained much attention as promiscuous biocatalysts showing good levels of reactivity in C-C bond formation, C-heteroatom bond formation, oxidative processes, and novel hydrolytic reactions. This critical review covers recent investigation in the field of catalytic promiscuity, and highlights the most surprising and uncommon activities that this class of enzymes shows in organic synthetic transformations (111 references).

Candida antarctica lipase B (CAL-B) is a very effective catalyst for the production of amines and amides using different enzymatic procedures. Simplicity of use, low cost, commercial availability and recycling possibility make this lipase an ideal tool for the synthesis and resolution of a wide range of nitrogenated compounds that can be used for the production of pharmaceuticals and interesting manufactures in the industrial sector.

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A one-pot/two-step chemoenzymatic sequential methodology has been developed for the selective amination of secondary alcohols by combining the laccase from Trametes versicolor/TEMPO catalytic system with the stereoselective action of transaminases.

Abstract. An efficient catalytic system to oxidize quantitatively aliphatic diols using Trametes versicolor laccase and TEMPO has been developed in aqueous medium. Oxidations have occurred in a non-stereoselective fashion but with complete regio-and/or monoselectivity, obtaining lactones with excellent purity after simple extraction. This catalytic system has been demonstrated to be scalable, compatible with the presence of a variety of functionalities, and also allowing the successful enzyme recycling using a laccase-CLEA preparation.