Comparative genomic analysis of azasugar biosynthesis
Azasugars are monosaccharide analogs in which the ring oxygen is replaced with a nitrogen atom. These well-known glycosidase inhibitors are of interest as therapeutics, yet several aspects of azasugars remain unknown including their distribution, structural diversity, and chemical ecology. The hallm...
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Published in | AMB Express Vol. 11; no. 1; p. 120 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Berlin/Heidelberg
Springer Berlin Heidelberg
23.08.2021
Springer Nature B.V SpringerOpen |
Subjects | |
Online Access | Get full text |
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Summary: | Azasugars are monosaccharide analogs in which the ring oxygen is replaced with a nitrogen atom. These well-known glycosidase inhibitors are of interest as therapeutics, yet several aspects of azasugars remain unknown including their distribution, structural diversity, and chemical ecology. The hallmark signature of bacterial azasugar biosynthesis is a three gene cluster (3GC) coding for aminotransferase, phosphatase, and dehydrogenase enzymes. Using the bioinformatics platform Enzyme Similarity Tool (EST), we identified hundreds of putative three gene clusters coding for azasugar production in microbial species. In the course of this work, we also report a consensus sequence for the aminotransferase involved in azasugar biosynthesis as being: SGNXFRXXXFPNXXXXXXXLXVPXPYCXRC. Most clusters are found in
Bacillus
and
Streptomyces
species which typically inhabit soil and the rhizosphere, but some clusters are found with diverse species representation such as
Photorhabdus
and
Xenorhabdus
which are symbiotic with entomopathogenic nematodes; the human skin commensal
Cutibacterium acnes,
and the marine
Bacillus rugosus
SPB7, a symbiont to the sea sponge
Spongia officinalis
. This pan-taxonomic survey of the azasugar 3GC signature may lead to the identification of new azasugar producers, facilitate studies of their natural functions, and lead to new potential therapeutics. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 2191-0855 2191-0855 |
DOI: | 10.1186/s13568-021-01279-5 |