title: Terpene synthases are widely distributed in bacteria.
abstract: Odoriferous terpene metabolites of bacterial origin have been known for many years. In genome-sequenced Streptomycetaceae microorganisms, the vast majority produces the degraded sesquiterpene alcohol geosmin. Two minor groups of bacteria do not produce geosmin, with one of these groups instead producing other sesquiterpene alcohols, whereas members of the remaining group do not produce any detectable terpenoid metabolites. Because bacterial terpene synthases typically show no significant overall sequence similarity to any other known fungal or plant terpene synthases and usually exhibit relatively low levels of mutual sequence similarity with other bacterial synthases, simple correlation of protein sequence data with the structure of the cyclized terpene product has been precluded. We have previously described a powerful search method based on the use of hidden Markov models (HMMs) and protein families database (Pfam) search that has allowed the discovery of monoterpene synthases of bacterial origin. Using an enhanced set of HMM parameters generated using a training set of 140 previously identified bacterial terpene synthase sequences, a Pfam search of 8,759,463 predicted bacterial proteins from public databases and in-house draft genome data has now revealed 262 presumptive terpene synthases. The biochemical function of a considerable number of these presumptive terpene synthase genes could be determined by expression in a specially engineered heterologous Streptomyces host and spectroscopic identification of the resulting terpene products. In addition to a wide variety of terpenes that had been previously reported from fungal or plant sources, we have isolated and determined the complete structures of 13 previously unidentified cyclic sesquiterpenes and diterpenes.
authors.affiliation: Laboratory of Microbial Engineering, Kitasato Institute for Life Sciences, Kitasato University, Kanagawa 252-0373, Japan;
authors.forename: Yuuki
authors.initials: Y
authors.lastname: Yamada
authors.affiliation: Biotechnology Research Center, University of Tokyo, Tokyo 113-8657, Japan;
authors.forename: Tomohisa
authors.initials: T
authors.lastname: Kuzuyama
authors.affiliation: Laboratory of Microbial Engineering, Kitasato Institute for Life Sciences, Kitasato University, Kanagawa 252-0373, Japan;
authors.forename: Mamoru
authors.initials: M
authors.lastname: Komatsu
authors.affiliation: National Institute of Advanced Industrial Science and Technology, Tokyo 135-0064, Japan;
authors.forename: Kazuo
authors.initials: K
authors.lastname: Shin-Ya
authors.affiliation: Laboratory of Microbial Engineering, Kitasato Institute for Life Sciences, Kitasato University, Tokyo 108-8461, Japan; and omuras@insti.kitasato-u.ac.jp ikeda@ls.kitasato-u.ac.jp.
authors.forename: Satoshi
authors.initials: S
authors.lastname: Omura
authors.affiliation: Department of Chemistry, Brown University, Providence, RI 02912-9108.
authors.forename: David E
authors.initials: DE
authors.lastname: Cane
authors.affiliation: Laboratory of Microbial Engineering, Kitasato Institute for Life Sciences, Kitasato University, Kanagawa 252-0373, Japan; omuras@insti.kitasato-u.ac.jp ikeda@ls.kitasato-u.ac.jp.
authors.forename: Haruo
authors.initials: H
authors.lastname: Ikeda
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D008390:Markov Chains
chemical_list: D019883:Alkyl and Aryl Transferases; C108877:terpene synthase
keywords: bacteria; heterologous expression; terpene synthase