ArticleFEBS open bio2026
Identifying and characterising a plant GH1 β-glucosidase that exhibits hydrolytic activity on N-linked glucopyranoside.
Article in FEBS open bio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
β-Glucosidases (Bgls) catalyse the hydrolysis of β-D-glycosidic bonds and are widely exploited as industrial biocatalysts. While their activity on O- and S-linked glycopyranosides is well established, hydrolysis of N-linked glycopyranosides by Bgls has not previously been demonstrated. Here, we screened a eukaryotic Bgl library for activity on methyl anthranilate-N-β-D-glucopyranoside (MANT-N-glucose), a novel N-glucopyranoside we recently produced biocatalytically. We identify ZmGlu1 as capable of hydrolysing this substrate, albeit with substantially reduced catalytic efficiency relative to native O-glucopyranoside substrates. Structural modelling of the enzyme-substrate complex reveals interactions likely underlying this reduced activity. These findings establish N-glycopyranosides as Bgl substrates and lay the groundwork for engineering Bgls with broader glycosidic bond specificity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.