Preprint Review Version 1 This version is not peer-reviewed

Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis

Version 1 : Received: 20 September 2019 / Approved: 21 September 2019 / Online: 21 September 2019 (01:28:13 CEST)

A peer-reviewed article of this Preprint also exists.

Shah, M.V.; Antoney, J.; Kang, S.W.; Warden, A.C.; Hartley, C.J.; Nazem-Bokaee, H.; Jackson, C.J.; Scott, C. Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis. Catalysts 2019, 9, 868. Shah, M.V.; Antoney, J.; Kang, S.W.; Warden, A.C.; Hartley, C.J.; Nazem-Bokaee, H.; Jackson, C.J.; Scott, C. Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis. Catalysts 2019, 9, 868.

Journal reference: Catalysts 2019, 9, 868
DOI: 10.3390/catal9100868

Abstract

Asymmetric reduction of enoates, imines and ketones are among the most important reactions in biocatalysis. These reactions are routinely conducted using enzymes that use nicotinamide cofactors as reductants. The deazaflavin cofactor F420 also has electrochemical properties that make it suitable as an alternative to nicotinamide cofactors for use in asymmetric reduction reactions. However, cofactor F420-dependent enzymes remain under-explored as a resource for biocatalysis. In this review, we consider the cofactor F420-dependent enzyme families with greatest potential for the discovery of new biocatalysts: the flavin/deazaflavin-dependent oxidoreductases (FDORs) and the luciferase-like hydride transferases (LLHTs). We discuss characterized F420-dependent reductions that have potential for adaptation for biocatalysis, and we consider the enzymes best suited for use in the reduction of oxidized cofactor F420 to allow cofactor recycling in situ. We also discuss recent advances in the production of cofactor F420 and its functional analog FO-5’- phosphate, which remains an impediment to the adoption of this family of enzymes for industrial biocatalytic processes. Finally, we discuss the prospects for the use of this cofactor and dependent enzymes as a resource for industrial biocatalysis.

Subject Areas

cofactor F420; deazaflavin; oxidoreductase; hydride transfer; hydrogenation; asymmetric synthesis; cofactor biosynthesis

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