Biology

Active site remodelling of a cyclodipeptide synthase redefines substrate scope

E. Sutherland, C. J. Harding, et al.

Discover how Emmajay Sutherland, Christopher John Harding, and Clarissa Melo Czekster have engineered cyclodipeptide synthases to produce valuable histidine-containing cyclic dipeptides. This groundbreaking research not only uncovers the histidine selection mechanism but also opens avenues for creating a diverse library of cyclic dipeptide analogs using various amino acids.

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Abstract

Cyclodipeptide synthases (CDPSs) generate cyclic dipeptides using aminoacylated tRNAs. Only two CDPSs are known to utilize histidine, producing bioactive molecules. This research developed an in vitro system to create a library of histidine-containing cyclic dipeptide analogs using various amino acids. The structure of a cyclo(His-Pro)-producing CDPS was determined, and mutagenesis revealed the histidine selection mechanism, leading to engineered variants capable of using phenylalanine and leucine. This work demonstrates the engineering of CDPSs to produce desired molecules.

Publisher

Communications Chemistry

Published On

May 17, 2022

Authors

Emmajay Sutherland, Christopher John Harding, Clarissa Melo Czekster

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