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

DPH1 Gene Mutations Identify a Candidate SAM Pocket in Radical Enzyme Dph1•Dph2 for Diphthamide Synthesis on EF2.

Biomolecules - 16 Nov 2023

Ütkür Koray, Schmidt Sarina, Mayer Klaus, Klassen Roland, Brinkmann Ulrich, Schaffrath Raffael

Abstract excerpt

In eukaryotes, the Dph1•Dph2 dimer is a non-canonical radical SAM enzyme. Using iron-sulfur (FeS) clusters, it cleaves the cosubstrate S-adenosyl-methionine (SAM) to form a 3-amino-3-carboxy-propyl (ACP) radical for the synthesis of diphthamide. The latter decorates a histidine residue on elongation factor 2 (EF2) conserved from archaea to yeast and humans and is important for accurate mRNA translation and...

Read the complete abstract on PubMed

Topics

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

Share to Histidine
Share to Minor Histocompatibility Antigens

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to S-Adenosylmethionine

Share to Saccharomyces cerevisiae

Share to Tumor Suppressor Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 38002337
DOI: 10.3390/biom13111655
PMCID: PMC10669111

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

DPH1 Gene Mutations Identify a Candidate SAM Pocket in Radical Enzyme Dph1•Dph2 for Diphthamide Synthesis on EF2.PMID 38002337Read ↗

<em>DPH1 </em>Gene Mutations Identify a Candidate SAM Pocket in Radical Enzyme Dph1•Dph2 for Diphthamide Synthesis on EF2Semantic proximity Read ↗

Functional Integrity of Radical SAM Enzyme Dph1•Dph2 Requires Non-canonical Cofactor Motifs with Tandem CysteinesSemantic proximity Read ↗

The amidation step of diphthamide biosynthesis in yeast requires DPH6, a gene identified through mining the DPH1-DPH5 interaction network.Semantic proximity Read ↗

DPH1 and DPH2 variants that confer susceptibility to diphthamide deficiency syndrome in human cells and yeast models.Semantic proximity Read ↗

Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2.Semantic proximity Read ↗

Insights into diphthamide, key diphtheria toxin effector.Semantic proximity Read ↗

Conserved electron donor complex Dre2-Tah18 is required for ribonucleotide reductase metallocofactor assembly and DNA synthesis.Semantic proximity Read ↗

Deadenylation and Decapping Factors Cooperatively Stimulate Biochemical Activities of DEAD-Box ATPase Dhh1Semantic proximity Read ↗

Crystal structures of SAMHD1 inhibitor complexes reveal the mechanism of water-mediated dNTP hydrolysis.Semantic proximity Read ↗

Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis.Semantic proximity Read ↗

Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development.Semantic proximity Read ↗

Radical S-Adenosylmethionine Enzymes in Human Health and Disease.Semantic proximity Read ↗

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