ArticlePloS one2016
Using the Amino Acid Network to Modulate the Hydrolytic Activity of β-Glycosidases.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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
8 citing papers in PubMed, 22 citations in OpenAlex.
- A general model for analysis of linear and hyperbolic enzyme inhibition mechanisms.FEBS open bio · 2026Article
- Electrostatic potential as a reactivity scoring function in computer-assisted enzyme engineering.The FEBS journal · 2025Article
- Article
- Structural basis of EHEP-mediated offense against phlorotannin-induced defense from brown algae to protecteLife · 2023Article
- Mechanism of imidazole inhibition of a GH1 β-glucosidase.FEBS open bio · 2023Article
- Biochemical and Structural Analysis of a Glucose-Tolerant β-Glucosidase from the Hemicellulose-DegradingMolecules (Basel, Switzerland) · 2022Article
- Homodimerization of a glycoside hydrolase family GH1 β-glucosidase suggests distinct activity of enzyme different states.Protein science : a publication of the Protein Society · 2020Article
- Mutations close to a hub residue affect the distant active site of a GH1 β-glucosidase.PloS one · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The active site residues in GH1 β-glycosidases are compartmentalized into 3 functional regions, involved in catalysis or binding of glycone and aglycone motifs from substrate. However, it still remains unclear how residues outside the active site modulate the enzymatic activity. To tackle this question, we solved the crystal structure of the GH1 β-glycosidase from Spodoptera frugiperda (Sfβgly) to systematically map its residue contact network and correlate effects of mutations within and outside the active site. External mutations neighbouring the functional residues involved in catalysis and glycone-binding are deleterious, whereas mutations neighbouring the aglycone-binding site are less detrimental or even beneficial. The large dataset of new and previously characterized Sfβgly mutants supports that external perturbations are coherently transmitted to active site residues possibly through contacts and specifically disturb functional regions they interact to, reproducing the effects observed for direct mutations of functional residues. This allowed us to suggest that positions related to the aglycone-binding site are preferential targets for introduction of mutations aiming to further improve the hydrolytic activity of β-glycosidases.
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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.