Mechanistic Characterization of Two Chimeric Sesterterpene Synthases from Penicillium

Takaaki Mitsuhashi; Jan Rinkel; Masahiro Okada; Ikuro Abe; Jeroen S Dickschat

doi:10.1002/chem.201702766

Mechanistic Characterization of Two Chimeric Sesterterpene Synthases from Penicillium

Chemistry. 2017 Jul 26;23(42):10053-10057. doi: 10.1002/chem.201702766. Epub 2017 Jul 3.

Authors

Takaaki Mitsuhashi¹, Jan Rinkel², Masahiro Okada¹, Ikuro Abe¹, Jeroen S Dickschat²

Affiliations

¹ Graduate School of Pharmaceutical Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
² Kekulé-Institute of Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Straße 1, 53121, Bonn, Germany.

PMID: 28671289
DOI: 10.1002/chem.201702766

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.

MeSH terms

Alkyl and Aryl Transferases / chemistry
Alkyl and Aryl Transferases / metabolism*
Cyclization
Dimethylallyltranstransferase / chemistry
Dimethylallyltranstransferase / metabolism
Magnetic Resonance Spectroscopy
Molecular Conformation
Penicillium / classification
Penicillium / enzymology*
Sesterterpenes / biosynthesis
Sesterterpenes / chemistry

Substances

Sesterterpenes
Alkyl and Aryl Transferases
terpene synthase
Dimethylallyltranstransferase