What to sacrifice? Fusions of cofactor regenerating enzymes with Baeyer-Villiger monooxygenases and alcohol dehydrogenases for self-sufficient redox biocatalysis

TETRAHEDRON

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Article

Mourelle-Insua, Angela¹  Aalbers, Friso S.²  Lavandera, Ivan¹  Gotor-Fernandez, Vicente¹  Fraaije, Marco W.² 

[1] Univ Oviedo, Dept Quim Organ & Inorgan, Lab Quim Bioorgan, Ave Julian Claveria 8, E-33006 Oviedo, Spain

[2] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Mol Enzymol Grp, Nijenborgh 4, NL-9747 AG Groningen, Netherlands

关键词: Cofactor recycling;    Enzyme fusion;    Self-sufficient enzyme;    Alcohol dehydrogenase;    Baeyer-Villiger monooxygenase;    Enantioselective;   

DOI  :  10.1016/j.tet.2019.02.015

来源: Elsevier

【 摘 要 】

A collection of fusion biocatalysts has been generated that can be used for self-sufficient oxygenations or ketone reductions. These biocatalysts were created by fusing a Baeyer-Villiger monooxygenase (cyclohexanone monooxygenase from Thermocrispum municipale: TmCHMO) or an alcohol dehydrogenase (alcohol dehydrogenase from Lactobacillus brevis: LbADH) with three different cofactor regeneration enzymes (formate dehydrogenase from Burkholderia stabilis: BsFDH; glucose dehydrogenase from Sulfolobus tokodaii: StGDH, and phosphite dehydrogenase from Pseudomonas stutzeri: PsPTDH). Their tolerance against various organic solvents, including a deep eutectic solvent, and their activity and selectivity with a variety of substrates have been studied. Excellent conversions and enantioselectivities were obtained, demonstrating that these engineered fusion enzymes can be used as biocatalysts for the synthesis of (chiral) valuable compounds. (C) 2019 The Authors. Published by Elsevier Ltd.

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