Evidence map›Paper›PMID 22093698›Full record

ArticleArchives of biochemistry and biophysics2012

New insights into the metabolism of organomercury compounds: mercury-containing cysteine S-conjugates are substrates of human glutamine transaminase K and potent inactivators of cystathionine γ-lyase.

Christy C Bridges, Boris F Krasnikov, Lucy Joshee, John T Pinto, André Hallen, Jianyong Li, Rudolfs K Zalups, Arthur J L Cooper

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.5field-weighted citation impact, top 32% 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

17 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Hydrogen Sulfide (HCurrent neuropharmacology · 2022
    Review
  10. Sulfhydryl groups as targets of mercury toxicity.Coordination chemistry reviews · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Neurodevelopmental Effects of Mercury.Advances in neurotoxicology · 2018
    Article
  17. Comparative enzymology of (2S,4R)4-fluoroglutamine and (2S,4R)4-fluoroglutamate.Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology · 2012
    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

8 authors at 4 institutions in 2 countries.

Christy C BridgesDivision of Basic Medical Sciences, Mercer University School of Medicine, Macon, GA 31207, USA.
Boris F Krasnikov
Lucy Joshee
John T Pinto
André Hallen
Jianyong Li
Rudolfs K Zalups
Arthur J L Cooper
Mercer University · USNew York Medical College · USMacquarie University · AUVirginia Tech · US

Funding

MECHANISM OF GLUTATHIONE CONJUGATE DEPENDENT TOXICITYR01ES008421 · NIEHS · WINIFRED MASTERSON BURKE MED RES INST · PI COOPER, ARTHUR JOSEPH · 1997 to 2007
$2.0M
TRANSPORT-TOXICITY OF INORGANIC MERCURY IN THE NEPHRONR01ES005980 · NIEHS · MERCER UNIVERSITY MACON · PI ZALUPS, RUDOLFS KARLIS · 1993 to 2006
$1.7M
METALLOTHIONEIN, MERCURY AND MONOCYTE ACTIVATIONR01ES011288 · NIEHS · MERCER UNIVERSITY MACON · PI ZALUPS, RUDOLFS KARLIS · 2002 to 2006
$1.5M
Targets for selenium in prostate cancer preventionR01CA111842 · NCI · WINIFRED MASTERSON BURKE MED RES INST · PI PINTO, JOHN T · 2006 to 2009
$1.2M
Kynurenic Acid Synthesis in Mouse BrainR01NS062836 · NINDS · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI LI, JIANYONG · 2009 to 2010
$851k
Proximal Tubular Transport of Mercury and Effects of Reduced Renal MassR15ES019991 · NIEHS · MERCER UNIVERSITY MACON · PI BRIDGES, CHRISTY C · 2011 to 2011
$471k
Role of Multidrug Resistance Proteins 2 and/or 4, and DMPS and DMSA in the RenalR03ES015511 · NIEHS · MERCER UNIVERSITY MACON · PI BRIDGES, CHRISTY C · 2007 to 2008
$145k
NCI NIH HHS CA111842NCI NIH HHS R01 CA111842NIEHS NIH HHS R01 ES005980NIEHS NIH HHS R01 ES008421NIEHS NIH HHS R01 ES011288NIEHS NIH HHS R01 ES11288NIEHS NIH HHS R01 ES5980NIEHS NIH HHS R01 ES8421NIEHS NIH HHS R03 ES015511NIEHS NIH HHS R03 ES15511NIEHS NIH HHS R15 ES019991NIEHS NIH HHS R15 ES19991NINDS NIH HHS NS062836NINDS NIH HHS R01 NS062836
6 · The paper itself

Abstract

Anthropogenic practices and recycling in the environment through natural processes result in release of potentially harmful levels of mercury into the biosphere. Mercury, especially organic forms, accumulates in the food chain. Mercury reacts readily with sulfur-containing compounds and often exists as a thiol S-conjugate, such as the l-cysteine (Cys)-S-conjugate of methylmercury (CH(3)Hg-S-Cys) or inorganic mercury (Cys-S-Hg-S-Cys). These S-conjugates are structurally similar to l-methionine and l-cystine/l-cystathionine, respectively. Bovine and rat glutamine transaminase K (GTK) catalyze transamination of sulfur-containing amino acids. Recombinant human GTK (rhGTK) has a relatively open catalytic active site, and we report here that this enzyme, like the rat and bovine enzymes, can also utilize sulfur-containing l-amino acids, including l-methionine, l-cystine, and l-cystathionine as substrates. The current study extends this list to include mercuric S-conjugates, and shows that CH(3)Hg-S-Cys and Cys-S-Hg-S-Cys are substrates and reversible inhibitors of rhGTK. The homocysteine S-conjugates, Hcy-S-Hg-S-Hcy and CH(3)Hg-S-Hcy, are also inhibitors. Finally, we show that HgCl(2), CH(3)Hg-S-Cys and Cys-S-Hg-S-Cys are potent irreversible inhibitors of rat cystathionine γ-lyase. The present study broadens our knowledge of the biochemistry of mercury compounds by showing that Cys S-conjugates of mercury interact with enzymes that catalyze transformations of biologically important sulfur-containing amino acids.

Indexed as

Amino Acids, SulfurAnimalsCattleCystathionine gamma-LyaseCysteineCystineHumansLyasesMercuric ChlorideMethylmercury CompoundsModels, MolecularOrganomercury CompoundsRatsRecombinant ProteinsSubstrate SpecificitySulfhydryl Compounds2-amino-3-(2-amino-2-carboxyethylsulfanyl-mercuricsulfanyl)-propionic acidAmino Acids, SulfurCystathionine gamma-LyaseCysteineCystineglutamine - phenylpyruvate transaminaseLyasesMercuric ChlorideMethylmercury CompoundsOrganomercury CompoundsRecombinant ProteinsSulfhydryl CompoundsTransaminases

Identifiers

PMID22093698
PMCPMC3246031
OpenAlexW2055702882

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.