type	Journal Article
authors	Ushimaru R, Liu HW.
title	Biosynthetic Origin of the Atypical Stereochemistry in the Thioheptose Core of Albomycin Nucleoside Antibiotics
journal	J Am Chem Soc
Activity	abmd
Family	abmd
sel	selected
ui	30673214.1
year	(2019)
volume	141
number	6
pages	2211-2214
keywords	doi: 10.1021/jacs.8b12565
abstract	Albomycins are peptidyl thionucleoside natural products that display antimicrobial activity against clinically important patho-gens. Their structures are characterized by a thioheptose with atypical stereochemistry including a D-xylofuranose ring modified with a D-amino acid moiety. Herein it is demonstrated that AbmH is a pyridoxal 5'-phosphate (PLP)-dependent transal-dolase that catalyzes a threo-selective aldol-type reaction to gener-ate the thioheptose core with a D-ribofuranose ring and an L-amino acid moiety. The conversion of L- to D-amino acid con-figuration is catalyzed by the PLP-dependent epimerase AbmD. The D-ribo to D-xylo conversion of the thiofuranose ring appears according to gene deletion experiments to be mediated by AbmJ, which is annotated as a radical S-adenosyl-L-methionine (SAM) enzyme. These studies establish several key steps in the as-sembly of the thioheptose core during the biosynthesis of albomycins.
last changed	2019/03/12 09:52