Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutation of a pH-modulating residue in a GH51 α-l-arabinofuranosidase leads to a severe reduction of the secondary hydrolysis of transfuranosylation products.

Biochimica et biophysica acta - 1 Jan 2014

Bissaro Bastien, Saurel Olivier, Arab-Jaziri Faten, Saulnier Luc, Milon Alain, Tenkanen Maija, Monsan Pierre, O'Donohue Michael J, Fauré Régis

Abstract excerpt

BACKGROUND: The development of enzyme-mediated glycosynthesis using glycoside hydrolases is still an inexact science, because the underlying molecular determinants of transglycosylation are not well understood. In the framework of this challenge, this study focused on the family GH51 α-l-arabinofuranosidase from Thermobacillus xylanilyticus, with the aim to understand why the mutation of position 344 provokes a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Arabinose
Share to Bacillaceae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to Chromatography, Thin Layer

Share to Glycoside Hydrolases

Share to Glycosylation

Share to Hydrolysis

Share to Magnetic Resonance Spectroscopy

Source

Identifiers

PMID: 24140392
DOI: 10.1016/j.bbagen.2013.10.013

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutation of a pH-modulating residue in a GH51 α-l-arabinofuranosidase leads to a severe reduction of the secondary hydrolysis of transfuranosylation products.PMID 24140392Read ↗

Probing the determinants of the transglycosylation/hydrolysis partition in a retaining α-l-arabinofuranosidase.Semantic proximity Read ↗

Enhancing the chemoenzymatic synthesis of arabinosylated xylo-oligosaccharides by GH51 α-L-arabinofuranosidase.Semantic proximity Read ↗

Modulation of the Activity and Regioselectivity of a Glycosidase: Development of a Convenient Tool for the Synthesis of Specific Disaccharides.Semantic proximity Read ↗

Probing the catalytically essential residues of the alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus.Semantic proximity Read ↗

Eliminating hydrolytic activity without affecting the transglycosylation of a GH1 β-glucosidase.Semantic proximity Read ↗

Functional roles of H98 and W99 and β2α2 loop dynamics in the α-l-arabinofuranosidase from Thermobacillus xylanilyticus.Semantic proximity Read ↗

Semi-rational approach for converting a GH1 β-glycosidase into a β-transglycosidase.Semantic proximity Read ↗

Probing impact of active site residue mutations on stability and activity of Neisseria polysaccharea amylosucrase.Semantic proximity Read ↗

Biochemical identification of the catalytic residues of a glycoside hydrolase family 120 β-xylosidase, involved in xylooligosaccharide metabolisation by gut bacteria.Semantic proximity Read ↗

Modulating Glycoside Hydrolase Activity between Hydrolysis and Transfer Reactions Using an Evolutionary Approach.Semantic proximity Read ↗

Rational design of Bacillus stearothermophilus US100 L-arabinose isomerase: potential applications for D-tagatose production.Semantic proximity Read ↗

A transitional hydrolase to glycosynthase mutant by Glu to Asp substitution at the catalytic nucleophile in a retaining glycosidase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.