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Biosynthesis of the Carbonylmethylene Structure Found in the Ketomemicin Class of Pseudotripeptides
Author(s) -
Kawata Junpei,
Naoe Taiki,
Ogasawara Yasushi,
Dairi Tohru
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201611005
Subject(s) - dehydratase , biosynthesis , stereochemistry , chemistry , isostere , heterologous expression , biochemistry , amide , aldolase a , biology , enzyme , gene , recombinant dna
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.