open access

https://hdl.handle.net/2115/68303

Biosynthesis of the Carbonylmethylene Structure Found in the Ketomemicin Class of Pseudotripeptides

英語

pseudopeptides

2017-02-13

Wiley-Blackwell

Angewandte chemie-international edition

56(8)

2026-2029

We recently discovered novel pseudotripeptides, the ketomemicins, which possess a C-terminal pseudodipeptide connected with a carbonylmethylene instead of an amide bond, through heterologous expression of gene clusters identified in actinobacteria. The carbonylmethylene structure is a stable isostere of the amide bond and its biological significance has been shown in several natural and synthetic products. Despite the biological importance of these compounds, little is known about how the carbonylmethylene structure is biosynthesized. In this work, we fully characterized the biosynthetic machinery of the pseudodipeptide. An aldolase, dehydratase, PLP-dependent glycine-C-acetyltransferase, and dehydrogenase were involved in the formation of the pseudodipeptide, with malonyl-CoA and phenylpyruvate as starter substrates.

学術雑誌論文

Accepted Manuscript

This is the peer reviewed version of the following article: Angewandte Chemie International Edition　Volume 56, Issue 8　February 13, 2017 , which has been published in final form at http://onlinelibrary.wiley.com/doi/10.1002/anie.201611005/abstract. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.

1433-7851