Exploring the substrate scope of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae.

ABSTRACT: Ferulic acid decarboxylase from Saccharomyces cerevisiae (ScFDC1) was described to possess a novel, prenylated flavin mononucleotide cofactor (prFMN) providing the first enzymatic 1,3-dipolar cycloaddition mechanism. The high tolerance of the enzyme towards several non-natural substrates, combined with its high quality, atomic resolution structure nominates FDC1 an ideal candidate as flexible biocatalyst for decarboxylation reactions leading to synthetically valuable styrenes. Herein the substrate scope of ScFDC1 is explored on substituted cinnamic acids bearing different functional groups (-OCH₃, -CF₃ or -Br) at all positions of the phenyl ring (o-, m-, p-)_, as well as on several biaryl and heteroaryl cinnamic acid analogues or derivatives with extended al

SUBMITTER: Nagy EZA 

PROVIDER: S-EPMC6345843 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature