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

Alteration of the flexible loop in 1-deoxy-D-xylulose-5-phosphate reductoisomerase boosts enthalpy-driven inhibition by fosmidomycin.

Biochemistry - 3 Jun 2014

Kholodar Svetlana A, Tombline Gregory, Liu Juan, Tan Zhesen, Allen C Leigh, Gulick Andrew M, Murkin Andrew S

Abstract excerpt

1-Deoxy-d-xylulose-5-phosphate reductoisomerase (DXR), which catalyzes the first committed step in the 2-C-methyl-d-erythritol 4-phosphate pathway of isoprenoid biosynthesis used by Mycobacterium tuberculosis and other infectious microorganisms, is absent in humans and therefore an attractive drug target. Fosmidomycin is a nanomolar inhibitor of DXR, but despite great efforts, few analogues with comparable...

Read the complete abstract on PubMed

Topics

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

Share to Aldose-Ketose Isomerases
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Fosfomycin

Share to Hydrogen Bonding

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 24825256
DOI: 10.1021/bi5004074
PMCID: PMC4045324

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Alteration of the flexible loop in 1-deoxy-D-xylulose-5-phosphate reductoisomerase boosts enthalpy-driven inhibition by fosmidomycin.PMID 24825256Read ↗

Resistance to the antimicrobial agent fosmidomycin and an FR900098 prodrug through mutations in the deoxyxylulose phosphate reductoisomerase gene (dxr).Semantic proximity Read ↗

Identification of a 1-deoxy-D-xylulose-5-phosphate synthase (DXS) mutant with improved crystallographic properties.Semantic proximity Read ↗

1-Deoxy- <scp>d</scp> -Xylulose 5-Phosphate Reductoisomerase (IspC) from <i>Mycobacterium tuberculosis</i> : towards Understanding Mycobacterial Resistance to FosmidomycinSemantic proximity Read ↗

Kinetic Characterization and Phosphoregulation of the Francisella tularensis 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase (MEP Synthase)Semantic proximity Read ↗

Aromatic residues in mobile regions distal to the active site support the closed conformation of <i>E. coli</i> DXPSSemantic proximity Read ↗

Isolation of Genomic Deoxyxylulose Phosphate Reductoisomerase (DXR) Mutations Conferring Resistance to FosmidomycinSemantic proximity Read ↗

A computational study of the molecular basis of antibiotic resistance in a DXR mutant.Semantic proximity Read ↗

Functional roles of H98 and W99 and β2α2 loop dynamics in the α-l-arabinofuranosidase from Thermobacillus xylanilyticus.Semantic proximity Read ↗

Differential local stability governs the metamorphic fold-switch of bacterial virulence factor RfaHSemantic proximity Read ↗

Water-mediated network in the resistance mechanism of fosfomycin.Semantic proximity Read ↗

The designability of protein switches by chemical rescue of structure: mechanisms of inactivation and reactivation.Semantic proximity Read ↗

Dynamics-based protein network features accurately discriminate neutral and rheostat positions.Semantic proximity Read ↗

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