Bacterial polysaccharide lyase family 33: Specificity from an evolutionarily conserved binding tunnel Article Swipe
Mélanie Loiodice
,
Élodie Drula
,
Zak McIver
,
S.V. Antonyuk
,
Arnaud Baslé
,
Marcelo A. Lima
,
Edwin A. Yates
,
Dominic P. Byrne
,
Jamie Coughlan
,
Andrew Leech
,
Shahram Mesdaghi
,
Daniel J. Rigden
,
Sophie Drouillard
,
William Helbert
,
Bernard Henrissat
,
Nicolas Terrapon
,
Gareth S. A. Wright
,
Marie Couturier
,
Alan Cartmell
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1073/pnas.2421623122
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1073/pnas.2421623122
Acidic glycans are essential for the biology of multicellular eukaryotes. To utilize them, microbial life including symbionts and pathogens has evolved polysaccharide lyases (PL) that cleave their 1,4 glycosidic linkages via a β-elimination mechanism. PL family 33 (PL33) enzymes have the unusual ability to target a diverse range of glycosaminoglycans (GAGs), as well as the bacterial polymer, gellan gum. In order to gain more detailed insight into PL33 activities we recombinantly expressed 10 PL33 members derived from all major environments and further elucidated the detailed biochemical and biophysical properties of five, showing that their substrate specificity is conferred by variations in tunnel length and topography. The key amino acids involved in catalysis and substrate interactions were identified, and employing a combination of complementary biochemical, structural, and modeling approaches, we show that the tunnel topography is induced by substrate binding to the glycan. Structural and bioinformatic analyses revealed that these features are conserved across several lyase families as well as in mammalian GAG epimerases.
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Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1073/pnas.2421623122
- OA Status
- hybrid
- Cited By
- 3
- References
- 52
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4407370373
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4407370373Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1073/pnas.2421623122Digital Object Identifier
- Title
-
Bacterial polysaccharide lyase family 33: Specificity from an evolutionarily conserved binding tunnelWork title
- Type
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articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
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2025Year of publication
- Publication date
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2025-02-11Full publication date if available
- Authors
-
Mélanie Loiodice, Élodie Drula, Zak McIver, S.V. Antonyuk, Arnaud Baslé, Marcelo A. Lima, Edwin A. Yates, Dominic P. Byrne, Jamie Coughlan, Andrew Leech, Shahram Mesdaghi, Daniel J. Rigden, Sophie Drouillard, William Helbert, Bernard Henrissat, Nicolas Terrapon, Gareth S. A. Wright, Marie Couturier, Alan CartmellList of authors in order
- Landing page
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https://doi.org/10.1073/pnas.2421623122Publisher landing page
- Open access
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YesWhether a free full text is available
- OA status
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hybridOpen access status per OpenAlex
- OA URL
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https://doi.org/10.1073/pnas.2421623122Direct OA link when available
- Concepts
-
Glycan, Glycosidic bond, Cleave, Lyase, Substrate specificity, Biochemistry, Glycobiology, Polysaccharide, Enzyme, Biology, Multicellular organism, Chemistry, Gene, GlycoproteinTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
3Total citation count in OpenAlex
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2025: 3Per-year citation counts (last 5 years)
- References (count)
-
52Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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