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Updated: Jun 17, 2026

Enzymatic Cascade Reactions for the Synthesis of Chiral Amino Alcohols from L-lysine
Published on: February 16, 2018
Biosynthesis of dihydrochalcomycin: characterization of a deoxyallosyltransferase (gerGTI)
Binod Babu Pageni1, Dinesh Simkhada, Tae-Jin Oh
1Institute of Biomolecule Reconstruction, Department of Pharmaceutical Engineering, Sun Moon University, Asan 336-708, Korea.
Abstract:
Through an inactivation experiment followed by complementation, the gerGTII gene was previously characterized as a chalcosyltransferase gene involved in the biosynthesis of dihydochalcomycin. The glycosyltransferase gerGTI was identified as a deoxyallosyltransferase required for the glycosylation of D-mycinose sugar. This 6-deoxyhexose sugar was converted to mycinose, via bis-O-methylation, following attachment to the polyketide lactone during dihydrochalcomycin biosynthesis. Gene sequence alignment of gerGTI to several glycosyltransferases revealed a consensus sequence motif that appears to be characteristic of the enzymes in this sub-group of the glycosyltransferase family. To characterize its putative function, genetic disruption of gerGTI in the wild-type strain Streptomyces sp. KCTC 0041BP and in the gerGTII-deleted mutant (S. sp. Delta gerGTsss, as well as complementation of gerGTII in S. sp. Delta gerGTss-GTs, were carried out, and the products were analyzed by LC/MS. S. sp. Delta gerGTss-GTs mutant produced dihydrochalconolide macrolide. S. sp. Delta gerGTs and S. sp. Delta gerGTss-GTs complementation of gerGTII yielded dihydrochalconolide without the mycinose sugar. The intermediate shows that gerGTI encodes a deoxyallosyltransferase that acts after gerGTII.
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