Evidence map›Paper›PMID 17921290›Full record

ArticleJournal of bacteriology2007

Characterization of the Mycobacterium tuberculosis 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase: potential for drug development.

Hyungjin Eoh, Amanda C Brown, Lori Buetow, William N Hunter, Tanya Parish, Devinder Kaur, Patrick J Brennan, Dean C Crick

Abstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
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  4. Metabolite Dysregulation by Pranlukast inMolecules (Basel, Switzerland) · 2022
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  12. Biochemistry of the non-mevalonate isoprenoid pathway.Cellular and molecular life sciences : CMLS · 2011
    Review
  13. Article
  14. Article
  15. Article
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  19. Article
  20. A triclinic crystal form of Escherichia coli 4-diphosphocytidyl-2C-methyl-D-erythritol kinase and reassessment of the quaternary structure.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    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 3 institutions in 2 countries.

Hyungjin EohMycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523, USA.
Amanda C Brown
Lori Buetow
William N Hunter
Tanya Parish
Devinder Kaur
Patrick J Brennan
Dean C Crick
Colorado State University · USQueen Mary University of London · GBUniversity of Dundee · GB

Funding

Vascular stabilization as a broad theraprutic platform for biodefenseU54AI065357 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · PI SLAYDEN, RICHARD A · 2005 to 2013
$77.5M
TUBERCULOSIS RESEARCH MATERIALS AND VACINE TESTINGN01AI075320 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · 1997 to 2004
$980k
Biotechnology and Biological Sciences Research Council BB/D000181/1NIAID NIH HHS AI-065357NIAID NIH HHS N01-AI-75320NIAID NIH HHS U54 AI065357
6 · The paper itself

Abstract

Mycobacterium tuberculosis utilizes the methylerythritol phosphate (MEP) pathway for biosynthesis of isopentenyl diphosphate and its isomer, dimethylallyl diphosphate, precursors of all isoprenoid compounds. This pathway is of interest as a source of new drug targets, as it is absent from humans and disruption of the responsible genes has shown a lethal phenotype for Escherichia coli. In the MEP pathway, 4-diphosphocytidyl-2-C-methyl-D-erythritol is formed from 2-C-methyl-D-erythritol 4-phosphate (MEP) and CTP in a reaction catalyzed by a 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase (IspD). In the present work, we demonstrate that Rv3582c is essential for M. tuberculosis: Rv3582c has been cloned and expressed, and the encoded protein has been purified. The purified M. tuberculosis IspD protein was capable of catalyzing the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol in the presence of MEP and CTP. The enzyme was active over a broad pH range (pH 6.0 to 9.0), with peak activity at pH 8.0. The activity was absolutely dependent upon divalent cations, with 20 mM Mg2+ being optimal, and replacement of CTP with other nucleotide 5'-triphosphates did not support activity. Under the conditions tested, M. tuberculosis IspD had Km values of 58.5 microM for MEP and 53.2 microM for CTP. Calculated kcat and kcat/Km values were 0.72 min(-1) and 12.3 mM(-1) min(-1) for MEP and 1.0 min(-1) and 18.8 mM(-1) min(-1) for CTP, respectively.

Indexed as

Cations, DivalentCloning, MolecularCoenzymesCytidine TriphosphateEnzyme StabilityErythritolEscherichia coliGene ExpressionGenes, EssentialHydrogen-Ion ConcentrationKineticsMycobacterium tuberculosisNucleotidyltransferasesRecombinant ProteinsSubstrate SpecificitySugar Phosphates2-C-methylerythritol 4-phosphate4-diphosphocytidyl-2-C-methylerythritol4-diphosphocytidyl-2-C--methylerythritol synthaseCations, DivalentCoenzymesCytidine TriphosphateErythritolNucleotidyltransferasesRecombinant ProteinsSugar Phosphates

Identifiers

PMID17921290
PMCPMC2168624
OpenAlexW2146971411

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.