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

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

Scientific reports - 23 Oct 2015

Madhuprakash Jogi, Bobbili Kishore Babu, Moerschbacher Bruno M, Singh Tej Pal, Swamy Musti J, Podile Appa Rao

Abstract excerpt

Serratia proteamaculans chitinase-D (SpChiD) has a unique combination of hydrolytic and transglycosylation (TG) activities. The TG activity of SpChiD can be used for large-scale production of chito-oligosaccharides (CHOS). The multiple activities (hydrolytic and/or chitobiase activities and TG) of SpChiD appear to be strongly influenced by the substrate-binding cleft. Here, we report the unique property of SpChiD...

Read the complete abstract on PubMed

Topics

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

Share to Acetylglucosaminidase
Share to Amino Acid Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chitinases

Share to Enzyme Stability

Share to Glycosylation

Share to Molecular Sequence Data

Share to Protein Binding

Share to Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 26493546
DOI: 10.1038/srep15657
PMCID: PMC4616163

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical analyses.PMID 26493546Read ↗

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

Active-site mutations improved the transglycosylation activity of Stenotrophomonas maltophilia chitinase A.Semantic proximity Read ↗

Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation.Semantic proximity Read ↗

Selection and mutational analyses of the substrate interacting residues of a chitinase from Enterobacter cloacae subsp. cloacae (EcChi2) to improve transglycosylation.Semantic proximity Read ↗

Fungal chitinases: diversity, mechanistic properties and biotechnological potential.Semantic proximity Read ↗

Thermostability Engineering of a Chitin-Utilizing GlcNAc Deacetylase from Acinetobacter baumannii via Distal Mutations.Semantic proximity Read ↗

Auxiliary active site mutations enhance the glycosynthase activity of a GH18 chitinase for polymerization of chitooligosaccharides.Semantic proximity Read ↗

Modulation of the transglycosylation activity of plant family GH18 chitinase by removing or introducing a tryptophan side chain.Semantic proximity Read ↗

Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with the Aspergillus fumigatus AfChiB1.Semantic proximity Read ↗

Structural analysis of group II chitinase (ChtII) catalysis completes the puzzle of chitin hydrolysis in insects.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 ↗

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