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

Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants.

Biochemistry - 21 Mar 2006

Cetinbaş Naniye, Macauley Matthew S, Stubbs Keith A, Drapala Robert, Vocadlo David J

Abstract excerpt

O-GlcNAcase is a family 84 beta-N-acetylglucosaminidase catalyzing the hydrolytic cleavage of beta-O-linked 2-acetamido-2-deoxy-d-glycopyranose (O-GlcNAc) from serine and threonine residues of posttranslationally modified proteins. O-GlcNAcases use a double-displacement mechanism involving formation and breakdown of a transient bicyclic oxazoline intermediate. The key catalytic residues of any family 84 enzyme...

Read the complete abstract on PubMed

Topics

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

Share to Acetylglucosaminidase
Share to Aspartic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Azides

Share to beta-N-Acetylhexosaminidases

Share to Catalysis

Share to Histone Acetyltransferases

Share to Hydrogen-Ion Concentration

Share to Multienzyme Complexes

Source

Identifiers

PMID: 16533067
DOI: 10.1021/bi052370b

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

Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants.PMID 16533067Read ↗

Efficient glycosynthase mutant derived from Mucor hiemalis endo-beta-N-acetylglucosaminidase capable of transferring oligosaccharide from both sugar oxazoline and natural N-glycan.Semantic proximity Read ↗

Structural basis for the inactivity of human blood group O2 glycosyltransferase.Semantic proximity Read ↗

Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase.Semantic proximity Read ↗

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

Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase.Semantic proximity Read ↗

Golgi alpha-mannosidase II cleaves two sugars sequentially in the same catalytic site.Semantic proximity Read ↗

CRISPR-Cas9-mediated depletion of <i>O</i> -GlcNAc hydrolase and transferase for functional dissection of <i>O</i> -GlcNAcylation in human cellsSemantic proximity Read ↗

An Enzymatic Toolkit for Selective Proteolysis, Detection, and Visualization of Mucin-Domain GlycoproteinsSemantic proximity Read ↗

Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids.Semantic proximity Read ↗

Flexibility and mutagenic resiliency of glycosyltransferases.Semantic proximity Read ↗

Identification of catalytically important residues in the active site of Escherichia coli transaldolase.Semantic proximity Read ↗

Highly conserved cysteines of mouse core 2 beta1,6-N-acetylglucosaminyltransferase I form a network of disulfide bonds and include a thiol that affects enzyme activity.Semantic proximity Read ↗

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