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

Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo-1,4-beta-glucanases.

Biochemistry - 6 May 2008

Rudsander Ulla J, Sandstrom Corine, Piens Kathleen, Master Emma R, Wilson David B, Brumer Iii Harry, Kenne Lennart, Teeri Tuula T

Abstract excerpt

1H NMR spectroscopy has been used to analyze the product profiles arising from the hydrolysis of cellooligosaccharides by family GH9 cellulases. The product profiles obtained with the wild type and several active site mutants of a bacterial processive endoglucanase, TfCel9A, were compared with th...

Read the complete abstract on PubMed

Topics

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

Share to Actinomycetales
Share to Cellulase
Share to Hydrolysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Magnetic Resonance Spectroscopy

Share to Molecular Structure

Share to Oligosaccharides

Share to Populus

Source

Identifiers

PMID: 18402467
DOI: 10.1021/bi702193e

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18402467-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo-1,4-beta-glucanases.PMID 18402467Read ↗

Evolution of glucuronoxylan side chain variability in vascular plants and the counter-adaptation of pathogenic cell-wall-degrading hydrolasesSemantic proximity Read ↗

Structural basis of product inhibition by arabinose and xylose of the thermostable GH43 β-1,4-xylosidase from Geobacillus thermoleovorans IT-08.Semantic proximity Read ↗

Functional and modular analyses of diverse endoglucanases from Ruminococcus albus 8, a specialist plant cell wall degrading bacterium.Semantic proximity Read ↗

Genomics insights into different cellobiose hydrolysis activities in two Trichoderma hamatum strains.Semantic proximity Read ↗

N-Linked glycans are an important component of the processive machinery of cellobiohydrolases.Semantic proximity Read ↗

Towards understanding the role of membrane-bound endo-beta-1,4-glucanases in cellulose biosynthesis.Semantic proximity Read ↗

Molecular Dynamics Simulations of Family 7 Cellobiohydrolase Mutants Aimed at Reducing Product Inhibition.Semantic proximity Read ↗

The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism.Semantic proximity Read ↗

Proton-Detected Solid-State NMR for Deciphering Structural Polymorphism and Dynamic Heterogeneity of Cellular Carbohydrates in Pathogenic FungiSemantic proximity Read ↗

Understanding The Structure And Composition of Recalcitrant Oligosaccharides In Ammonia Treated Lignocellulosic Biomass Hydrolysate Using High-Throughput Biotin- Based Glycome Profiling And Mass Spectrometry.Semantic proximity Read ↗

Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D.Semantic proximity Read ↗

Mutant barley (1-->3,1-->4)-beta-glucan endohydrolases with enhanced thermostability.Semantic proximity Read ↗

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