Evidence map›Paper›PMID 19413286›Full record

ArticleBiochemistry2009

Human glyoxalase II contains an Fe(II)Zn(II) center but is active as a mononuclear Zn(II) enzyme.

Pattraranee Limphong, Ross M McKinney, Nicole E Adams, Brian Bennett, Christopher A Makaroff, Thusitha Gunasekera, Michael W Crowder

Abstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.4field-weighted citation impact, top 14% 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

8 citing papers in PubMed, 28 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Pattraranee LimphongDepartment of Chemistry and Biochemistry, 160 Hughes Hall, Miami University, Oxford, Ohio 45056, USA.
Ross M McKinney
Nicole E Adams
Brian Bennett
Christopher A Makaroff
Thusitha Gunasekera
Michael W Crowder
Miami University · USMedical College of Wisconsin · US

Funding

TR&D Project 3P41EB001980 · NIBIB · MEDICAL COLLEGE OF WISCONSIN · PI KLUG, CANDICE S · 2003 to 2017
$16.3M
Substrate &Inhibitor Binding in Leucine AminopeptidaseR01AI056231 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI BENNETT, BRIAN · 2003 to 2007
$923k
Arabidopsis AtETHE1, A model to understand the metabolic role of ETHE1R15GM076199 · NIGMS · MIAMI UNIVERSITY OXFORD · PI MAKAROFF, CHRISTOPHER A · 2008 to 2008
$213k
NIAID NIH HHS AI056231NIAID NIH HHS R01 AI056231NIBIB NIH HHS EB001980NIBIB NIH HHS P41 EB001980NIGMS NIH HHS GM076199-01A2NIGMS NIH HHS R15 GM076199
6 · The paper itself

Abstract

Human glyoxalase II (Glx2) was overexpressed in rich medium and in minimal medium containing zinc, iron, or cobalt, and the resulting Glx2 analogues were characterized using metal analyses, steady-state and pre-steady-state kinetics, and NMR and EPR spectroscopies to determine the nature of the metal center in the enzyme. Recombinant human Glx2 tightly binds nearly 1 equiv each of Zn(II) and Fe. In contrast to previous reports, this study demonstrates that an analogue containing 2 equiv of Zn(II) cannot be prepared. EPR studies suggest that most of the iron in recombinant Glx2 is Fe(II). NMR studies show that Fe(II) binds to the consensus Zn(2) site in Glx2 and that this site can also bind Co(II) and Ni(II), suggesting that Zn(II) binds to the consensus Zn(1) site. The NMR studies also reveal the presence of a dinuclear Co(II) center in Co(II)-substituted Glx2. Steady-state and pre-steady-state kinetic studies show that Glx2 containing only 1 equiv of Zn(II) is catalytically active and that the metal ion in the consensus Zn(2) site has little effect on catalytic activity. Taken together, these studies suggest that Glx2 contains a Fe(II)Zn(II) center in vivo but that the catalytic activity is due to Zn(II) in the Zn(1) site.

Indexed as

Binding SitesCatalytic DomainCobaltElectron Spin Resonance SpectroscopyHumansHydroxyacylglutathione HydrolaseIronKineticsModels, BiologicalModels, MolecularRecombinant ProteinsThiolester HydrolasesZincCobaltHydroxyacylglutathione HydrolaseIronRecombinant ProteinsThiolester HydrolasesZinc

Identifiers

PMID19413286
PMCPMC4627686
OpenAlexW1966265281

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.