Evidence map›Paper›PMID 21447318›Full record

ArticleAnalytical biochemistry2011

Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes.

Stephanie Wickham, Matthew B West, Paul F Cook, Marie H Hanigan

Abstract read
In one paragraph

Article in Analytical biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed, 2 pooled it
1.6field-weighted citation impact, top 19% 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

63 citing papers in PubMed, 2 syntheses or guidelines pooled it, 130 citations in OpenAlex.

  1. Pooled it
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  6. HyperpolarizedACS sensors · 2026
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3 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Stephanie WickhamDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
Matthew B West
Paul F Cook
Marie H Hanigan
University of Oklahoma Health Sciences Center · USUniversity of Oklahoma · US

Funding

SIGNIFICANCE OF GGT EXPRESSION IN TUMORSR01CA057530 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HANIGAN, MARIE H · 1992 to 2008
$1.9M
Significance of GGT Expression in TumorsR56CA057530 · NCI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI HANIGAN, MARIE H · 2009 to 2009
$238k
NCI NIH HHS R01 CA057530NCI NIH HHS R01CA57530NCI NIH HHS R56 CA057530NCI NIH HHS R56CA57530
6 · The paper itself

Abstract

Gamma-glutamyl compounds include antioxidants, inflammatory molecules, drug metabolites, and neuroactive compounds. Two cell surface enzymes that metabolize gamma-glutamyl compounds have been identified: gamma-glutamyl transpeptidase (GGT1) and gamma-glutamyl leukotrienase (GGT5). There is controversy in the literature regarding the substrate specificity of these enzymes. To address this issue, we have developed a method for comprehensive kinetic analysis of compounds as substrates for GGT enzymes. Our assay is sensitive, quantitative, and conducted at physiological pH. We evaluated a series of gamma-glutamyl compounds as substrates for human GGT1 and human GGT5. The K(m) value for reduced glutathione was 11μM for both GGT1 and GGT5. However, the K(m) values for oxidized glutathione were 9μM for GGT1 and 43μM for GGT5. Our data show that the K(m) values for leukotriene C(4) are equivalent for GGT1 and GGT5 at 10.8 and 10.2μM, respectively. This assay was also used to evaluate serine-borate, a well-known inhibitor of GGT1, which was 8-fold more potent in inhibiting GGT1 than in inhibiting GGT5. These data provide essential information regarding the target enzymes for developing treatments for inflammatory diseases such as asthma and cardiovascular disease in humans. This assay is invaluable for studies of oxidative stress, drug metabolism, and other pathways that involve gamma-glutamyl compounds.

Indexed as

DipeptidasesEnzyme Assaysgamma-GlutamyltransferaseGlutamic AcidGlutathioneHumansKineticsLeukotriene C4Substrate SpecificityDipeptidasesgamma-glutamyl leukotrienasegamma-GlutamyltransferaseGlutamic AcidGlutathioneLeukotriene C4

Identifiers

PMID21447318
PMCPMC3099546
OpenAlexW1989344941

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.