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Glycosyltransferases are a very important class of enzymes which can be found in biosynthetic gene clusters of a variety of natural compounds. Some of these GTs show a remarkable flexibility towards the donor and the acceptor molecules making them most valuable for combinatorial biosynthesis. Future work is expected to focus on learning more about sugar biosynthesis, sugar modification and sugar attachment to support in vivo engineering of novel natural products. [ABSTRACT FROM AUTHOR] more...

For the development and production of pharmacologically important compounds based on natural scaffolds simple and effective techniques that can combine chemistry, genetics and molecular biology are indispensable. The NRPSs can provide such interesting tools to generate and modify novel products. The recently gained structural and mechanistic information on NRPSs have made this class of multienzymes a powerful native tool box that would help to achieve this goal. Rearrangements of domains and modules in combination with the elucidation of chemoenzymatic reactions highly increases the potential of these special enzymes. [ABSTRACT FROM AUTHOR] more...

The modular structure of the multienzyme PKSs makes them particularly attractive targets for combinatorial biosynthesis aimed at generating novel polyketide medicines. We are beginning to understand those features of subunit organization and structure and their linking and docking elements, which are critical for productive engineering efforts. Although mechanistic and specificity studies have shown that natural PKS domains are generally not best-suited to serve as universal combinatorial units, recent insights such as those afforded by the mycolactone PKS should allow progress towards this goal. [ABSTRACT FROM AUTHOR] more...