3 years ago

Mechanistic Characterization of Two Chimeric Sesterterpene Synthases from Penicillium

Mechanistic Characterization of Two Chimeric Sesterterpene Synthases from Penicillium
Takaaki Mitsuhashi, Jeroen S. Dickschat, Masahiro Okada, Ikuro Abe, Jan Rinkel
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. The products and cyclization mechanisms of two bifunctional sesterterpene synthases from Penicillium were investigated. A phylogenetic analysis of the new and known fungal terpene synthases reveals clades of enzymes that reflect the initial cyclization step.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/chem.201702766

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