Activity and Biocatalytic Potential of an Indolylamide Generating Thioesterase.
Weimao Zhong, Zachary L Budimir, Lucas O Johnson, Elizabeth I Parkinson, Vinayak Agarwal
Author Information
Weimao Zhong: School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.
Zachary L Budimir: James Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, United States.
Lucas O Johnson: James Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, United States.
Elizabeth I Parkinson: James Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, United States. ORCID
Vinayak Agarwal: School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, United States. ORCID
The chemical synthesis of -acyl indoles is hindered by the poor nucleophilicity of indolic nitrogen, necessitating the use of strongly basic reaction conditions that encumber elaboration of highly functionalized scaffolds. Herein, we describe the total chemoenzymatic synthesis of the bulbiferamide natural products by the biochemical activity reconstitution of a nonribosomal peptide synthetase assembly line-derived (NRPS-derived) thioesterase that neatly installs the macrocyclizing indolylamide. The enzyme represents a starting point for biocatalytic access to macrocyclic indolylamide peptides and natural products.
