Evidence map›Paper›PMID 16227621›Full record

ArticleThe Journal of biological chemistry2005

Structural studies on a mitochondrial glyoxalase II.

Gishanthi P K Marasinghe, Ian M Sander, Brian Bennett, Gopalraj Periyannan, Ke-Wu Yang, Christopher A Makaroff, Michael W Crowder

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

42 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Applied and environmental microbiology · 2024
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  6. Review
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  11. Review
  12. Thioesterase enzyme families: Functions, structures, and mechanisms.Protein science : a publication of the Protein Society · 2022
    Article
  13. Review
  14. Dual Activity BLEG-1 fromInternational journal of molecular sciences · 2021
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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.

Gishanthi P K MarasingheDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, USA.
Ian M Sander
Brian Bennett
Gopalraj Periyannan
Ke-Wu Yang
Christopher A Makaroff
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
Characterization of Metallo-B-LactamasesR01GM067928 · NIGMS · MIAMI UNIVERSITY OXFORD · PI CROWDER, MICHAEL W · 2002 to 2005
$645k
NIAID NIH HHS AI056231NIAID NIH HHS R01 AI056231NIBIB NIH HHS EB001980NIBIB NIH HHS P41 EB001980NIGMS NIH HHS GM40075NIGMS NIH HHS R01 GM067928
6 · The paper itself

Abstract

Glyoxalase 2 is a beta-lactamase fold-containing enzyme that appears to be involved with cellular chemical detoxification. Although the cytoplasmic isozyme has been characterized from several organisms, essentially nothing is known about the mitochondrial proteins. As a first step in understanding the structure and function of mitochondrial glyoxalase 2 enzymes, a mitochondrial isozyme (GLX2-5) from Arabidopsis thaliana was cloned, overexpressed, purified, and characterized using metal analyses, EPR and (1)H NMR spectroscopies, and x-ray crystallography. The recombinant enzyme was shown to bind 1.04 +/- 0.15 eq of iron and 1.31 +/- 0.05 eq of Zn(II) and to exhibit k(cat) and K(m) values of 129 +/- 10 s(-1) and 391 +/- 48 microm, respectively, when using S-d-lactoylglutathione as the substrate. EPR spectra revealed that recombinant GLX2-5 contains multiple metal centers, including a predominant Fe(III)Z-n(II) center and an anti-ferromagnetically coupled Fe(III)Fe(II) center. Unlike cytosolic glyoxalase 2 from A. thaliana, GLX2-5 does not appear to specifically bind manganese. (1)H NMR spectra revealed the presence of at least eight paramagnetically shifted resonances that arise from protons in close proximity to a Fe(III)Fe(II) center. Five of these resonances arose from solvent-exchangeable protons, and four of these have been assigned to NH protons on metal-bound histidines. A 1.74-A resolution crystal structure of the enzyme revealed that although GLX2-5 shares a number of structural features with human GLX2, several important differences exist. These data demonstrate that mitochondrial glyoxalase 2 can accommodate a number of different metal centers and that the predominant metal center is Fe(III)Zn(II).

Indexed as

Amino Acid SequenceArabidopsisBinding SitesCloning, MolecularCrystallography, X-RayElectron Spin Resonance SpectroscopyGene ExpressionHumansHydroxyacylglutathione HydrolaseIronIsoenzymesKineticsMagnetic Resonance SpectroscopyMetalsMitochondriaModels, MolecularHydroxyacylglutathione HydrolaseIronIsoenzymesMetalsRecombinant ProteinsThiolester HydrolasesZinc

Identifiers

PMID16227621
PMCPMC1343529
OpenAlexW2154600206

What OpenQuestion holds

Textmetadata
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.