| Literature DB >> 28671289 |
Takaaki Mitsuhashi1, Jan Rinkel2, Masahiro Okada1, Ikuro Abe1, Jeroen S Dickschat2.
Abstract
The products of two bifunctional fungal sesterterpene synthases (StTPS), with prenyl transferase (PT) and terpene synthase (TPS) domains from Penicillium, were structurally characterized and their mechanisms studied in detail by labeling experiments. A phylogenetic analysis of the TPS domains of the new and previously characterized enzymes revealed six distinct clades. Enzymes from the same clade catalyze a common initial cyclization step, which suggests the potential for structural predictions from amino acid sequences.Keywords: biosynthesis; carbocations; enzyme mechanisms; isotopes; terpenes
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Year: 2017 PMID: 28671289 DOI: 10.1002/chem.201702766
Source DB: PubMed Journal: Chemistry ISSN: 0947-6539 Impact factor: 5.236