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

Probing the substrate specificity of Golgi alpha-mannosidase II by use of synthetic oligosaccharides and a catalytic nucleophile mutant.

Journal of the American Chemical Society - 16 Jul 2008

Zhong Wei, Kuntz Douglas A, Ember Brian, Singh Harminder, Moremen Kelley W, Rose David R, Boons Geert-Jan

Abstract excerpt

Inhibition of Golgi alpha-mannosidase II (GMII), which acts late in the N-glycan processing pathway, provides a route to blocking cancer-induced changes in cell surface oligosaccharide structures. To probe the substrate requirements of GMII, oligosaccharides were synthesized that contained an alp...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Crystallography, X-Ray
Share to Glycosylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mannose

Share to Mannosidases

Share to Oligosaccharides

Share to Structure-Activity Relationship

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 18558690
DOI: 10.1021/ja711248y
PMCID: PMC3982601

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18558690-2026-09-02.2. 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

Probing the substrate specificity of Golgi alpha-mannosidase II by use of synthetic oligosaccharides and a catalytic nucleophile mutant.PMID 18558690Read ↗

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

Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates.Semantic proximity Read ↗

Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase.Semantic proximity Read ↗

Substrate recognition and catalysis by GH47 α-mannosidases involved in Asn-linked glycan maturation in the mammalian secretory pathway.Semantic proximity Read ↗

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

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 ↗

Structure-based engineering of E. coli galactokinase as a first step toward in vivo glycorandomization.Semantic proximity Read ↗

Mutant analysis reveals an alternative pathway for N-linked glycosylation in Drosophila melanogaster.Semantic proximity Read ↗

Modulation of the Activity and Regioselectivity of a Glycosidase: Development of a Convenient Tool for the Synthesis of Specific Disaccharides.Semantic proximity Read ↗

N-glycan structures and downstream mannose-phosphorylation of plant recombinant human alpha-L-iduronidase: toward development of enzyme replacement therapy for mucopolysaccharidosis I.Semantic proximity Read ↗

Mechanism-based inhibitors of glycosidases: design and applications.Semantic proximity Read ↗

Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety.Semantic proximity Read ↗

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