Evidence map›Paper›PMID 29708734›Full record

ArticleBiochemistry2018

Noncanonical Radical SAM Enzyme Chemistry Learned from Diphthamide Biosynthesis.

Min Dong, Yugang Zhang, Hening Lin

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 31% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Pathways of thymidine hypermodification.Nucleic acids research · 2022
    Article
  5. Diphthamide promotes TOR signaling by increasing the translation of proteins in the TORC1 pathway.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. The asymmetric function of Dph1-Dph2 heterodimer in diphthamide biosynthesis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Min DongDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.ORCID 0000-0001-6655-2818
Yugang ZhangDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.
Hening LinDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.ORCID 0000-0002-0255-2701
Cornell University · USHoward Hughes Medical Institute · US

Funding

Diphthamide biosynthesisR01GM088276 · NIGMS · CORNELL UNIVERSITY · PI LIN, HENING · 2009 to 2017
$2.5M
NIGMS NIH HHS R01 GM088276
6 · The paper itself

Abstract

Radical S-adenosylmethionine (SAM) enzymes are a superfamily of enzymes that use SAM and reduced [4Fe-4S] cluster to generate a 5'-deoxyadenosyl radical to catalyze numerous challenging reactions. We have reported a type of noncanonical radical SAM enzymes in the diphthamide biosynthesis pathway. These enzymes also use SAM and reduced [4Fe-4S] clusters, but generate a 3-amino-3-carboxypropyl (ACP) radical to modify the substrate protein, translation elongation factor 2. The regioselective cleavage of a different C-S bond of the sulfonium center of SAM in these enzymes comparing to canonical radical SAM enzymes is intriguing. Here, we highlight some recent findings in the mechanism of these types of enzymes, showing that the diphthamide biosynthetic radial SAM enzymes bound SAM with a distinct geometry. In this way, the unique iron of the [4Fe-4S] cluster in the enzyme can only attack the carbon on the ACP group to form an organometallic intermediate. The homolysis of the organometallic intermediate releases the ACP radical and generates the EF2 radial.

Indexed as

Biosynthetic PathwaysHistidineIron-Sulfur ProteinsPyrococcus horikoshiiS-AdenosylmethionineSubstrate SpecificitydiphthamideHistidineIron-Sulfur ProteinsS-Adenosylmethionine

Identifiers

PMID29708734
PMCPMC6893904
OpenAlexW2802187948

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.