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

Structural and functional roles of glycosylation in fungal laccase from Lentinus sp.

PloS one - 1 Jan 2015

Maestre-Reyna Manuel, Liu Wei-Chun, Jeng Wen-Yih, Lee Cheng-Chung, Hsu Chih-An, Wen Tuan-Nan, Wang Andrew H-J, Shyur Lie-Fen

Abstract excerpt

Laccases are multi-copper oxidases that catalyze the oxidation of various organic and inorganic compounds by reducing O2 to water. Here we report the crystal structure at 1.8 Å resolution of a native laccase (designated nLcc4) isolated from a white-rot fungus Lentinus sp. nLcc4 is composed of thr...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Glycosylation
Share to Laccase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidation-Reduction

Share to Pichia

Share to Protein Conformation

Share to Recombinant Proteins

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Source

Open in PubMed Open full text

Identifiers

PMID: 25849464
DOI: 10.1371/journal.pone.0120601
PMCID: PMC4388643

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25849464-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional roles of glycosylation in fungal laccase from Lentinus sp.PMID 25849464Read ↗

Crystal Structures of the C-Glycosyltransferase UGT708C1 from Buckwheat Provide Insights into the Mechanism of C-Glycosylation.Semantic proximity Read ↗

Importance of a Laccase Gene (Lcc1) in the Development of Ganoderma tsugae.Semantic proximity Read ↗

Biodegradation of dyes and polyaromatic hydrocarbons by two allelic forms of Lentinula edodes laccase expressed from Pichia pastoris.Semantic proximity Read ↗

The laccase multi-gene family in Coprinopsis cinerea has seventeen different members that divide into two distinct subfamilies.Semantic proximity Read ↗

Identification of laccase-like multicopper oxidases from the pathogenic fungus Setosphaeria turcica and their expression pattern during growth and infectionSemantic proximity Read ↗

Bioinformatic analysis reveals high diversity of bacterial genes for laccase-like enzymes.Semantic proximity Read ↗

Functional analyses of laccase genes from Fusarium oxysporum.Semantic proximity Read ↗

Effects of active site cleft residues on oligosaccharide binding, hydrolysis, and glycosynthase activities of rice BGlu1 and its mutants.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 ↗

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

Biochemical and structural characterization of Penicillium purpurogenum α-D galactosidase: Binding of galactose to an alternative pocket may explain enzyme inhibition.Semantic proximity Read ↗

The catalytic properties of Thermus thermophilus SG0.5JP17-16 laccase were regulated by the conformational dynamics of pocket loop 6.Semantic proximity Read ↗

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