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

Structure and mechanism of action of an inverting mutant sialidase.

Biochemistry - 28 Jun 2005

Newstead Simon, Watson Jacqueline N, Knoll Tara L, Bennet Andrew J, Taylor Garry

Abstract excerpt

Mutagenesis of the conserved tyrosine (Y370) of the Micromonospora viridifaciens sialidase to small amino acids changes the mechanism of catalysis from retention of anomeric configuration to inversion [Watson, J. N., et al. (2003) Biochemistry 42, 12682-12690]. For the Y370G mutant enzyme-catalyzed hydrolysis of a series of aryl sialosides and 3'-sialyllactose, the derived Brønsted parameters (beta(lg)) on k(cat)...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Catalysis
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Molecular Structure

Share to Neuraminidase

Share to Structure-Activity Relationship

Share to Tyrosine

Source

Identifiers

PMID: 15966735
DOI: 10.1021/bi050517t

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure and mechanism of action of an inverting mutant sialidase.PMID 15966735Read ↗

Mutants of Micromonospora viridifaciens sialidase have highly variable activities on natural and non-natural substrates.Semantic proximity Read ↗

A sialyltransferase mutant with decreased donor hydrolysis and reduced sialidase activities for directly sialylating LewisX.Semantic proximity Read ↗

A sialidase mutant displaying trans-sialidase activity.Semantic proximity Read ↗

Modulation of substrate specificities of D-sialic acid aldolase through single mutations of Val-251.Semantic proximity Read ↗

Mechanistic study of CMP-Neu5Ac hydrolysis by α2,3-sialyltransferase from Pasteurella dagmatis.Semantic proximity Read ↗

A new sialidase mechanism: bacteriophage K1F endo-sialidase is an inverting glycosidase.Semantic proximity Read ↗

Structural basis for the delivery of activated sialic acid into Golgi for sialyationSemantic proximity Read ↗

Free-energy computations identify the mutations required to confer trans-sialidase activity into Trypanosoma rangeli sialidase.Semantic proximity Read ↗

Cooperativity of catalytic and lectin-like domain of <i>T. congolense</i> trans-sialidase modulates its catalytic activitySemantic proximity Read ↗

Loss-of-function mutation in bi-functional marine bacterial sialyltransferase.Semantic proximity Read ↗

Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex.Semantic proximity Read ↗

Design of Trypanosoma rangeli sialidase mutants with improved trans-sialidase activity.Semantic proximity Read ↗

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