ArticlemicroPublication biology2024
Identification and analysis of a unique group of glycoside hydrolase family 188 sequences with an altered sulfonate binding residue.
Article in microPublication biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Taxonomic, genomic, and ecological insights into a novel Flavobacteriaceae strain from coastal tidal flats.BMC microbiology · 2025Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sulfoquinovosyldiacylglycerol (SQDG) is a plant sulfolipid that plays a major role in the global sulfur cycle. Bacteria contain sulfoglycolytic pathways that are responsible for metabolizing SQDG which requires initial delipidation by a sulfolipase and sulfoquinovosidase (SQase). Recently, a new group of SQases was discovered and have been categorized in a separate glycoside hydrolase family (GH188). Here we have identified a subset of GH188s with an altered sulfonate binding residue. We found that these GH188s have a distinct dimer interface and are found in unique gene clusters that may represent new sulfoglycolytic pathways. Further investigation into these enzymes could broaden our understanding of this new glycoside hydrolase family and uncover diverse sulfoglycolytic pathways.
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Registered trials
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