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Condensing Enzymes from Pseudoalteromonadaceae for Prodiginine Synthesis
Author(s) -
Brass Hannah U. C.,
Klein Andreas S.,
Nyholt Silke,
Classen Thomas,
Pietruszka Jörg
Publication year - 2019
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.201900183
Subject(s) - biocatalysis , chemistry , substrate (aquarium) , enzyme , biosynthesis , catalysis , substrate specificity , stereochemistry , combinatorial chemistry , biochemistry , reaction mechanism , biology , ecology
Prodiginines are natural products that are produced by various microorganisms. As the biological activity of prodiginines varies depending on their structure, prodiginine derivatives are of interest. In order to extend the prodiginine structural diversity, new condensing enzyme homologs of PigC were analysed. The condensing enzyme PigC from S. marcescens catalyses the last step in prodiginine biosynthesis and accepts not only its natural substrate, but also synthetically produced monopyrroles. Still, the substrate spectrum of PigC is partially limited. In order to enable the biocatalytic production of new prodiginine derivatives, PigC homologs supplementing the substrate spectra of PigC are of interest. Two condensing enzymes homologs from two tambjamine producing Pseudoalteromonadaceae strains were analysed towards their catalytic ability to produce the structurally related prodiginines. Besides the investigation of their substrate spectrum and enzyme kinetic data, a preparative scale biocatalysis approach for the production of prodiginine derivatives was established, comparing different condensing enzymes.