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

Apparent Reversal of Allosteric Response in Mycobacterium tuberculosis MenD Reveals Links to Half-of-Sites Reactivity.

Chembiochem : a European journal of chemical biology - 1 Apr 2025

Ho Ngoc Anh Thu, Given Fiona M, Stanborough Tamsyn, Klein Michelle, Allison Timothy M, Bulloch Esther M M, Jiao Wanting, Johnston Jodie M

Abstract excerpt

Redox-active molecules play critical roles in various biological functions, including cellular respiration. In bacterial electron transport chains, menaquinones serve as key electron carriers. The first committed enzyme in the menaquinone biosynthesis pathway of Mycobacterium tuberculosis (Mtb), MenD, is allosterically inhibited by 1,4-dihydroxy-2-naphthoic acid (DHNA), the first redox-active metabolite in the...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Kinetics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Mycobacterium tuberculosis

Share to Naphthols

Share to Vitamin K 2

Source

Identifiers

PMID: 39945237
DOI: 10.1002/cbic.202400943

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Apparent Reversal of Allosteric Response in Mycobacterium tuberculosis MenD Reveals Links to Half-of-Sites Reactivity.PMID 39945237Read ↗

Allosteric regulation of menaquinone (vitamin K2) biosynthesis in the human pathogen Mycobacterium tuberculosisSemantic proximity Read ↗

Allosteric Regulation of Vitamin K2 Biosynthesis in a Human PathogenSemantic proximity Read ↗

A dynamical-nonequilibrium molecular dynamics (D-NEMD) alanine scanning approach for identifying allosteric positions in proteinsSemantic proximity Read ↗

Using substrate analogues to probe the kinetic mechanism and active site of Escherichia coli MenD.Semantic proximity Read ↗

Dynamical Responses Predict a Distal Site that Modulates Activity in an Antibiotic Resistance EnzymeSemantic proximity Read ↗

Mechanistic insights into the conformational changes and alterations in residual communications due to the mutations in the pncA Gene of Mycobacterium tuberculosis: A computational perspective for effective therapeutic solutions.Semantic proximity Read ↗

Identification of a Mycothiol-Dependent Nitroreductase from Mycobacterium tuberculosis.Semantic proximity Read ↗

Structural and functional determination of homologs of the Mycobacterium tuberculosis N-acetylglucosamine-6-phosphate deacetylase (NagA).Semantic proximity Read ↗

Partial Saturation of Menaquinone in <i>Mycobacterium tuberculosis</i>: Function and Essentiality of a Novel Reductase, MenJSemantic proximity Read ↗

Molecular Dynamics Assisted Mechanistic Study of Isoniazid-Resistance against Mycobacterium tuberculosis InhA.Semantic proximity Read ↗

Distinct Substrate and Intermediate Recognition via Mutation Effects on Mycobacterium tuberculosis Methionyl-tRNA Synthetase.Semantic proximity Read ↗

Triple Mycobacterial ATP-synthase mutations impedes Bedaquiline binding: Atomistic and structural perspectives.Semantic proximity Read ↗

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