New Paper in ACS Chemical Biology
A new manuscript by our group was just published in ACS Chemical Biology.
Ketoreductase (KR) domains, the first of the canonical reductive loop domains, play a key role in the processing of 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 side reactions and blockages on the PKS.
In this paper we investigate the substrate-dependent performance, partcularly the velocity and stereoselectivity, of various KR domains in reactions with synthetic substrate surrogates. We show that the influence of even small structural changes can be significant, suggesting a more intensive investigation of this aspect.
Congratulations to Marius for his hard and finally successful work on this.
Click here to access the paper.