title: Diversification of echinomycin molecular structure by way of chemoenzymatic synthesis and heterologous expression of the engineered echinomycin biosynthetic pathway.
abstract: Echinomycin, a bis-intercalator antitumor cyclic peptide, is biosynthesized by a unique nonribosomal peptide synthetase (NRPS). Successful heterologous expression of the whole gene cluster of echinomycin in Escherichia coli let us to investigate a further application of echinomycin NRPS. To construct a cyclic peptide library, our approach through both chemoenzymatic and rational genetic engineering has been successfully demonstrated. These achievements provided the further support that E. coli-based system can serve as a flexible yet robust platform for producing complex natural products and their analogs.
authors.affiliation: Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan. watanabe.kenji@gmail.com
authors.forename: Kenji
authors.initials: K
authors.lastname: Watanabe
authors.forename: Hiroki
authors.initials: H
authors.lastname: Oguri
authors.forename: Hideaki
authors.initials: H
authors.lastname: Oikawa
mesh_terms: D053898:Biosynthetic Pathways; D004448:Echinomycin / Q000096:biosynthesis* / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005818:Genetic Engineering / Q000379:methods*; D010453:Peptide Synthases / Q000378:metabolism
chemical_list: D004448:Echinomycin; D010453:Peptide Synthases; C104385:non-ribosomal peptide synthase