ArticleThe Journal of biological chemistry2017
Discovery of α-l-arabinopyranosidases from human gut microbiome expands the diversity within glycoside hydrolase family 42.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Cloning, Expression, Purification, and Characterization of a Novel β-Galactosidase/α-L-Arabinopyranosidase fromMolecules (Basel, Switzerland) · 2023Article
- Substrate recognition mode of a glycoside hydrolase family 42 β-galactosidase fromMicrobiome research reports · 2023Article
- Article
- Structure and evolution of the bifidobacterial carbohydrate metabolism proteins and enzymes.Biochemical Society transactions · 2021Review
- Crystal structure of a homotrimeric verrucomicrobialJournal of structural biology: X · 2021Article
- Structure and function ofThe Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes of the glycoside hydrolase family 42 (GH42) are widespread in bacteria of the human gut microbiome and play fundamental roles in the decomposition of both milk and plant oligosaccharides. All GH42 enzymes characterized so far have β-galactosidase activity. Here, we report the existence of a GH42 subfamily that is exclusively specific for α-l-arabinopyranoside and describe the first representative of this subfamily. We found that this enzyme (
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