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 kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism.

The Journal of biological chemistry - 12 Nov 2010

Litzinger Silke, Fischer Stefanie, Polzer Patrick, Diederichs Kay, Welte Wolfram, Mayer Christoph

Abstract excerpt

Three-dimensional structures of NagZ of Bacillus subtilis, the first structures of a two-domain β-N-acetylglucosaminidase of family 3 of glycosidases, were determined with and without the transition state mimicking inhibitor PUGNAc bound to the active site, at 1.84- and 1.40-Å resolution, respectively. The structures together with kinetic analyses of mutants revealed an Asp-His dyad involved in catalysis:...

Read the complete abstract on PubMed

Topics

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

Share to Acetylglucosamine
Share to Acetylglucosaminidase

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Aspartic Acid

Share to Bacillus subtilis

Share to Biocatalysis

Share to Histidine

Share to Hydrogen Bonding

Share to Sodium Azide

Source

Open in PubMed Open full text

Identifiers

PMID: 20826810
DOI: 10.1074/jbc.M110.131037
PMCID: PMC2975192

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism.PMID 20826810Read ↗

Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis.Semantic proximity Read ↗

Crystal structure of a mutant glycosylasparaginase shedding light on aspartylglycosaminuria-causing mechanism as well as on hydrolysis of non-chitobiose substrate.Semantic proximity Read ↗

Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540.Semantic proximity Read ↗

The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors.Semantic proximity Read ↗

Deciphering the molecular basis of the broad substrate specificity of alpha-glucosidase from Bacillus sp. SAM1606.Semantic proximity Read ↗

Crystal structure of asparagine 233-replaced cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011 determined at 1.9 A resolution.Semantic proximity Read ↗

Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase.Semantic proximity Read ↗

Paenibacillus sp. TS12 glucosylceramidase: kinetic studies of a novel sub-family of family 3 glycosidases and identification of the catalytic residues.Semantic proximity Read ↗

Structure, Substrate Complexation and Reaction Mechanism of Bacterial AsparaginasesSemantic proximity Read ↗

Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9A resolution.Semantic proximity Read ↗

Biochemical and structural insights into an allelic variant causing the lysosomal storage disorder - aspartylglucosaminuria.Semantic proximity Read ↗

Recharacterization of EmAGA, a Potential Candidate for Novel ALL Therapeutics.Semantic proximity Read ↗

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