News

A new manuscript by our group was just published in ACS Chemical Biology.

Ketoreductase (KR) domains are the first of the canonical reductive loop domains and play a key role in the assembly of polyketide backbones by polyketide synthases (PKS). Attempts of directed multimodular PKS engineering depend heavily on the functioning of this domain type in the context of individual (engineered) modules. Altered precursor structures can significantly influence the performance of these enzymes, which can result in undesired side reactions and blockages on the PKS.

In this paper we investigate the substrate-dependent performance, particularly the stereoselectivity, of various KR domains in reactions with synthetic substrate surrogates. Interestingsly, the influence of even small structural changes can be significant, suggesting a more intensive investigation of this aspect to enable better PKS engineering in the future.

Congratulations to Marius for his hard and finally successful work on this.

Click here to access the paper.