Fluorescent Mechanism-Based Probe for Aerobic Flavin-Dependent Enzyme Activity.

ABSTRACT: Diversity in non-ribosomal peptide and polyketide secondary metabolism is facilitated by interactions between biosynthetic domains with discrete monomer loading and their cognate tailoring enzymes, such as oxidation or halogenation enzymes. The cooperation between peptidyl carrier proteins and flavin-dependent enzymes offers a specialized strategy for monomer selectivity for oxidization of small molecules from within a complex cellular milieu. In an effort to study this process, we have developed fluorescent probes to selectively label aerobic flavin-dependent enzymes. Here we report the preparation and implementation of these tools to label oxidase, monooxygenase, and halogenase flavin-dependent enzymes.

SUBMITTER: McCulloch IP 

PROVIDER: S-EPMC5656434 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature