| Literature DB >> 29125678 |
Jan Rinkel1, Lukas Lauterbach1, Jeroen S Dickschat1.
Abstract
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 Mn2+ catalysis on the presence of Asp-217, a residue that is occupied by a highly conserved Glu in most other bacterial terpene synthases.Entities:
Keywords: biosynthesis; enzyme mechanisms; isotopes; metal cofactors; terpenes
Mesh:
Substances:
Year: 2017 PMID: 29125678 DOI: 10.1002/anie.201711142
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336