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

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

International journal of biological macromolecules - 15 Dec 2020

Mallakuntla Mohan Krishna, Vaikuntapu Papa Rao, Bhuvanachandra Bhoopal, Podile Appa Rao

Abstract excerpt

Transglycosylation (TG) by Enterobacter cloacae subsp. cloacae chitinase 2 (EcChi2) has been deciphered by site-directed mutagenesis. EcChi2 originally displayed feeble TG with chitin oligomer with a degree of polymerization (DP4), for a short duration. Based on the 3D modelling and molecular docking analyses, we altered the substrate interactions at the substrate-binding cleft, catalytic center, and catalytic...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Chitinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enterobacter cloacae

Share to Glycosylation

Share to Hydrolysis

Share to Molecular Docking Simulation

Share to Structural Homology, Protein

Share to Substrate Specificity

Source

Identifiers

PMID: 33096170
DOI: 10.1016/j.ijbiomac.2020.10.125

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Selection and mutational analyses of the substrate interacting residues of a chitinase from Enterobacter cloacae subsp. cloacae (EcChi2) to improve transglycosylation.PMID 33096170Read ↗

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

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

Enhancing the catalytic activity of a GH5 processive endoglucanase from Bacillus subtilis BS-5 by site-directed mutagenesis.Semantic proximity Read ↗

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

Functional insights into a peculiar tetra-modular LPMO from the human pathogen Enterobacter cloacaeSemantic proximity Read ↗

Engineering Bacterial Chitinases for Industrial Application: From Protein Engineering to Bacterial Strains Mutation! A Comprehensive Review of Physical, Molecular, and Computational Approaches.Semantic proximity Read ↗

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

An evolution-based designing and characterization of mutants of cyclomaltodextrinase: Molecular modeling and spectroscopic studies.Semantic proximity Read ↗

Comprehensive in silico structural-functional analysis of Enterobacter GH19 class I chitinase (chiRAM) gene: cloning and heterologous expressionSemantic proximity Read ↗

Mutational analysis of the binding affinity and transport activity for N-acetylglucosamine of the novel ABC transporter Ngc in the chitin-degrader Streptomyces olivaceoviridis.Semantic proximity Read ↗

Exo-beta-D-glucosaminidase from Amycolatopsis orientalis: catalytic residues, sugar recognition specificity, kinetics, and synergism.Semantic proximity Read ↗

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