The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerization, and catalysis.

ABSTRACT: The UbiD family of reversible decarboxylases act on aromatic, heteroaromatic, and unsaturated aliphatic acids and utilize a prenylated flavin mononucleotide (prFMN) as cofactor, bound adjacent to a conserved Glu-Arg-Glu/Asp ionic network in the enzyme's active site. It is proposed that UbiD activation requires oxidative maturation of the cofactor, for which two distinct isomers, prFMN^ketimine and prFMN^iminium, have been observed. It also has been suggested that only the prFMN^iminium form is relevant to catalysis, which requires transient cycloaddition between substrate and cofactor. Using Aspergillus niger Fdc1 as a model system, we reveal that isomerization of prFMN^iminium to prFMN^ketimine is a light-dependent process that is l

SUBMITTER: Bailey SS 

PROVIDER: S-EPMC5818171 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature