BioWF: A Naturally‐Fused, Di‐Domain Biocatalyst from Biotin Biosynthesis Displays an Unexpectedly Broad Substrate Scope

Abstract

Supporting information for this article is given via a link at the end of the document.

Versatile Chemo-Biocatalytic Cascade Driven by a Thermophilic and Irreversible C–C Bond-Forming α-Oxoamine Synthase

“…This substrate scope sets Th AOS apart from other wild-type AOS enzymes, which are typically highly substrate specific, especially for the AA susbtrate . Two recently published AOS biocatalysts, SxtA and Alb29, catalyzed 9 and 7 reactions, respectively, but only with one AA each ( l -Arg for SxtA and l -Glu for Alb29). , A more recent AOS biocatalyst, the fusion enzyme BioWF from Corynebacterium amycolatum , was reported to catalyze 12 unique reactions, mostly with l -Ala but also including two reactions with Gly and l -Ser . Therefore, it appears that Th AOS is unique in terms of the diversity of substrate acceptance for both AA and acyl-CoA thioester substrates.…”

“… 4 , 1 A more recent AOS biocatalyst, the fusion enzyme BioWF from Corynebacterium amycolatum , was reported to catalyze 12 unique reactions, mostly with l -Ala but also including two reactions with Gly and l -Ser. 19 Therefore, it appears that Th AOS is unique in terms of the diversity of substrate acceptance for both AA and acyl-CoA thioester substrates. We next characterized Th AOS thermostability, finding it stable at temperatures of up to 80 °C over 3 h ( Figure S4 ).…”