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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 2+ catalysis on the presence of Asp‐217, a residue that is occupied by a highly conserved Glu in most other bacterial terpene synthases.
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Rinkel et al. (2017) studied this question.
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