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Mechanistic Characterization of Two Chimeric Sesterterpene Synthases from Penicillium
Author(s) -
Mitsuhashi Takaaki,
Rinkel Jan,
Okada Masahiro,
Abe Ikuro,
Dickschat Jeroen S.
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201702766
Subject(s) - terpene , biology , enzyme , atp synthase , stereochemistry , clade , transferase , phosphofructokinase 2 , bifunctional , phylogenetic tree , biochemistry , chemistry , gene , catalysis
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.