|
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.
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last changed |
2019/03/12 09:52 |
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