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

Essential residues for the enzyme activity of ATP-dependent MurE ligase from Mycobacterium tuberculosis.

Protein & cell - 1 Nov 2010

Basavannacharya Chandrakala, Moody Paul R, Munshi Tulika, Cronin Nora, Keep Nicholas H, Bhakta Sanjib

Abstract excerpt

The emergence of total drug-resistant tuberculosis (TDRTB) has made the discovery of new therapies for tuberculosis urgent. The cytoplasmic enzymes of peptidoglycan biosynthesis have generated renewed interest as attractive targets for the development of new anti-mycobacterials. One of the cytopl...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Catalytic Domain
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Models, Molecular

Share to Mycobacterium tuberculosis

Share to Peptide Synthases

Share to Sequence Alignment

Source

Open in PubMed Open full text

Identifiers

PMID: 21153518
DOI: 10.1007/s13238-010-0132-9
PMCID: PMC3962982

Genes

DAP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21153518-2026-09-02.2. 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

Essential residues for the enzyme activity of ATP-dependent MurE ligase from Mycobacterium tuberculosis.PMID 21153518Read ↗

Cell wall peptidoglycan inMycobacterium tuberculosis: An Achilles’ heel for the TB-causing pathogenSemantic proximity Read ↗

Kinetic and mutational studies of the adenosine diphosphate ribose hydrolase from Mycobacterium tuberculosis.Semantic proximity Read ↗

Mycobacterium tuberculosis MutT1 (Rv2985) and ADPRase (Rv1700) proteins constitute a two-stage mechanism of 8-oxo-dGTP and 8-oxo-GTP detoxification and adenosine to cytidine mutation avoidance.Semantic proximity Read ↗

Crystal Structure and Biochemical Characterization of a Mycobacterium smegmatis AAA-Type Nucleoside Triphosphatase Phosphohydrolase (Msm0858).Semantic proximity Read ↗

A modified BCG with depletion of enzymes associated with peptidoglycan amidation induces enhanced protection against tuberculosis in miceSemantic proximity Read ↗

Structural basis for protein glutamylation by the Legionella pseudokinase SidJ.Semantic proximity Read ↗

NAD+-dependent DNA Ligase (Rv3014c) from Mycobacterium tuberculosis. Crystal structure of the adenylation domain and identification of novel inhibitors.Semantic proximity Read ↗

A modified BCG with depletion of enzymes associated with peptidoglycan amidation induces enhanced protection against tuberculosis in miceSemantic proximity Read ↗

The dUTPase enzyme is essential in Mycobacterium smegmatis.Semantic proximity Read ↗

Pyrimidine Salvage Pathway in Mycobacterium tuberculosisSemantic proximity Read ↗

Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA Synthetase (FadD13) of Mycobacterium tuberculosis.Semantic proximity Read ↗

Further Insight into S-Adenosylmethionine-dependent MethyltransferasesSemantic proximity Read ↗

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