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 of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin.

Biochimica et biophysica acta - 14 Jan 2004

Vaaje-Kolstad Gustav, Houston Douglas R, Rao Francesco V, Peter Martin G, Synstad Bjørnar, van Aalten Daan M F, Eijsink Vincent G H

Abstract excerpt

Catalysis by ChiB, a family 18 chitinase from Serratia marcescens, involves a conformational change of Asp142 which is part of a characteristic D(140)XD(142)XE(144) sequence motif. In the free enzyme Asp142 points towards Asp140, whereas it rotates towards the catalytic acid, Glu144, upon ligand...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Acetylglucosamine
Share to Binding, Competitive

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chitinases

Share to Enzyme Inhibitors

Share to Hydrogen-Ion Concentration

Share to Serratia marcescens

Share to Trisaccharides

Source

Identifiers

PMID: 14726210
DOI: 10.1016/j.bbapap.2003.09.014

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-14726210-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin.PMID 14726210Read ↗

Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone.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 ↗

The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism.Semantic proximity Read ↗

Importance of exposed aromatic residues in chitinase B from Serratia marcescens 2170 for crystalline chitin hydrolysis.Semantic proximity Read ↗

Key Residues Affecting Transglycosylation Activity in Family 18 Chitinases: Insights into Donor and Acceptor Subsites.Semantic proximity Read ↗

Family 18 chitinase-oligosaccharide substrate interaction: subsite preference and anomer selectivity of Serratia marcescens chitinase A.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 ↗

Development and application of a model for chitosan hydrolysis by a family 18 chitinase.Semantic proximity Read ↗

Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.Semantic proximity Read ↗

A DFT study of the unusual substrate-assisted mechanism of Serratia marcescens chitinase B reveals the role of solvent and mutational effect on catalysis.Semantic proximity Read ↗

Accessory active site residues of Streptomyces sp. N174 chitosanase: variations on a common theme in the lysozyme superfamily.Semantic proximity Read ↗

Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical analyses.Semantic proximity Read ↗

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