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

Analysis of the role of O-glycosylation in GH51 α-L-arabinofuranosidase from Pleurotus ostreatus.

Biotechnology and applied biochemistry - 1 Jan 2000

Amore Antonella, Serpico Annabel, Amoresano Angela, Vinciguerra Roberto, Faraco Vincenza

Abstract excerpt

In this study, the recombinant α-L-arabinofuranosidase from the fungus Pleurotus ostreatus (rPoAbf) was subjected to site-directed mutagenesis with the aim of elucidating the role of glycosylation on the properties of the enzyme at the level of S160 residue. As a matter of fact, previous mass spectral analyses had led to the localization of a single O-glycosylation at this site. Recombinant expression and...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Biocatalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Glycoside Hydrolases

Share to Glycosylation

Share to Molecular Sequence Data

Share to Mutation

Share to Pleurotus

Source

Open in PubMed Open full text

Identifiers

PMID: 25471797
DOI: 10.1002/bab.1325
PMCID: PMC5032992

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Analysis of the role of O-glycosylation in GH51 α-L-arabinofuranosidase from Pleurotus ostreatus.PMID 25471797Read ↗

Development of an improved variant of GH51 α-l-arabinofuranosidase from Pleurotus ostreatus by directed evolution.Semantic proximity Read ↗

Crystal structure of β-glucosidase 1A from Thermotoga neapolitana and comparison of active site mutants for hydrolysis of flavonoid glucosides.Semantic proximity Read ↗

Structural and biochemical analyses of β-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila involved in mucin degradation.Semantic proximity Read ↗

Mutational analysis of N-glycosylation recognition sites on the biochemical properties of Aspergillus kawachii alpha-L-arabinofuranosidase 54.Semantic proximity Read ↗

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

Structural Analysis of β-Fructofuranosidase from Xanthophyllomyces dendrorhous Reveals Unique Features and the Crucial Role of N-Glycosylation in Oligomerization and Activity.Semantic proximity Read ↗

Characterization of the O-Glycoproteome of Porphyromonas gingivalisSemantic proximity Read ↗

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

Crystal structure and characterization of the glycoside hydrolase family 62 α-L-arabinofuranosidase from Streptomyces coelicolor.Semantic proximity Read ↗

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

Knockout of an endogenous mannosyltransferase increases the homogeneity of glycoproteins produced in Pichia pastoris.Semantic proximity Read ↗

Effect of N-Linked Glycosylation of Recombinant Windmill Palm Tree Peroxidase on Its Activity and Stability.Semantic proximity Read ↗

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