A terpene synthase from the marine bacterium Streptomyces xinghaiensis has been characterised, including a full structure elucidation of its products from various substrates and an in-depth investigation of the enzyme mechanism by isotope labelling experiments, metal cofactor variations, and mutation experiments. The results revealed an interesting dependency of Mn catalysis on the presence of Asp-217, a residue that is occupied by a highly conserved Glu in most other bacterial terpene synthases.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1002/anie.201711142 | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!