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

Substitutions in an active site loop of Escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo.

The Journal of biological chemistry - 7 May 2004

Lauhon Charles T, Skovran Elizabeth, Urbina Hugo D, Downs Diana M, Vickery Larry E

Abstract excerpt

IscS catalyzes the fragmentation of l-cysteine to l-alanine and sulfane sulfur in the form of a cysteine persulfide in the active site of the enzyme. In Escherichia coli IscS, the active site cysteine Cys(328) resides in a flexible loop that potentially influences both the formation and stability...

Read the complete abstract on PubMed

Topics

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

Share to Carbon-Sulfur Lyases
Share to Hydro-Lyases
Share to Iron-Sulfur Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Chemical

Share to RNA, Transfer

Share to Subcellular Fractions

Share to Succinate Dehydrogenase

Share to Thionucleotides

Source

Identifiers

PMID: 14978044
DOI: 10.1074/jbc.M401261200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-14978044-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Substitutions in an active site loop of Escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo.PMID 14978044Read ↗

Structural alterations of the cysteine desulfurase IscS of Salmonella enterica serovar Typhimurium reveal substrate specificity of IscS in tRNA thiolation.Semantic proximity Read ↗

The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli.Semantic proximity Read ↗

Formation of thiolated nucleosides present in tRNA from Salmonella enterica serovar Typhimurium occurs in two principally distinct pathways.Semantic proximity Read ↗

Cysteine desulfurase (IscS)–mediated fine-tuning of bioenergetics and SUF expression prevents Mycobacterium tuberculosis hypervirulenceSemantic proximity Read ↗

Turning Escherichia coli into a Frataxin-Dependent Organism.Semantic proximity Read ↗

A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli.Semantic proximity Read ↗

The iron-binding CyaY and IscX proteins assist the ISC-catalyzed Fe-S biogenesis in Escherichia coli.Semantic proximity Read ↗

Site-specific mutational analysis of a novel cysteine motif proposed to ligate the 4Fe-4S cluster in the iron-sulfur flavoprotein of the thermophilic methanoarchaeon Methanosarcina thermophila.Semantic proximity Read ↗

Lack of YggX results in chronic oxidative stress and uncovers subtle defects in Fe-S cluster metabolism in Salmonella enterica.Semantic proximity Read ↗

Novel features of the ISC machinery revealed by characterization of Escherichia coli mutants that survive without iron-sulfur clusters.Semantic proximity Read ↗

The iscS gene deficiency affects the expression of pyrimidine metabolism genes.Semantic proximity Read ↗

The cysteine desulfurase IscS is required for synthesis of all five thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium.Semantic proximity Read ↗

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