Evidence map›Paper›PMID 26289554›Full record

ArticleChembiochem : a European journal of chemical biology2015

Characterization of Early Enzymes Involved in TDP-Aminodideoxypentose Biosynthesis en Route to Indolocarbazole AT2433.

Pauline Peltier-Pain, Shanteri Singh, Jon S Thorson

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. 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

3 authors.

Pauline Peltier-PainPharmaceutical Sciences Division, University of Wisconsin-Madison, 777 Highland Avenue, Madison, WI, 53705, USA.
Shanteri SinghCenter for Pharmaceutical Research and Innovation, Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Jon S ThorsonCenter for Pharmaceutical Research and Innovation, Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA. jsthorson@uky.edu.

Funding

Kentucky Center for Clinical and Translational ScienceUL1TR000117 · NCATS · UNIVERSITY OF KENTUCKY · PI KERN, PHILIP A · 2012 to 2015
$13.3M
WATER DISTRIB:PHYSICAL PROPERT:PIZZA &LMPS MOZZARELLA CHEESES:EARLY STAGE MATURP41RR002301 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 1985 to 2011
$13.0M
In Vitro Glycorandomization of Natural ProductsR37AI052218 · NIAID · UNIVERSITY OF KENTUCKY · PI THORSON, JON SCOTT · 2012 to 2021
$4.0M
STUDIES ON CALICHEAMICIN BIOSYNTHESIS AND SELF RESISTANCER01CA084374 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI THORSON, JON SCOTT · 2000 to 2013
$3.6M
WIDE-BORE 9.4 TESLA NMR SPECTROMETER FOR UW-MADISONS10RR002781 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1986 to 1986
–
CONSOLE UPGRADES FOR NMR FACILITYS10RR008438 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1993 to 1993
–
NCATS NIH HHS UL1 TR000117NCATS NIH HHS UL1TR 000117NCI NIH HHS R01 CA084374NCI NIH HHS R01 CA84374NCRR NIH HHS P41 RR002301NCRR NIH HHS P41RR02301NCRR NIH HHS S10 RR002781NCRR NIH HHS S10 RR008438NIAID NIH HHS R37 AI052218PHS HHS P41M10399
6 · The paper itself

Abstract

The characterization of TDP-α-D-glucose dehydrogenase (AtmS8), TDP-α-D-glucuronic acid decarboxylase (AtmS9), and TDP-4-keto-α-D-xylose 2,3-dehydratase (AtmS14), involved in Actinomadura melliaura AT2433 aminodideoxypentose biosynthesis, is reported. This study provides the first biochemical evidence that both deoxypentose and deoxyhexose biosynthetic pathways share common strategies for sugar 2,3-dehydration/reduction and implicates the sugar nucleotide base specificity of AtmS14 as a potential mechanism for sugar nucleotide commitment to secondary metabolism. In addition, a re-evaluation of the AtmS9 homologue involved in calicheamicin aminodeoxypentose biosynthesis (CalS9) reveals that CalS9 catalyzes UDP-4-keto-α-D-xylose as the predominant product, rather than UDP-α-D-xylose as previously reported. Cumulatively, this work provides additional fundamental insights regarding the biosynthesis of novel pentoses attached to complex bacterial secondary metabolites.

Indexed as

CarbazolesGlucose 1-DehydrogenaseGlutamate DecarboxylaseHydro-LyasesMolecular StructureNucleoside Diphosphate SugarsProton Magnetic Resonance SpectroscopyCarbazolesGlucose 1-DehydrogenaseGlutamate DecarboxylaseHydro-LyasesNucleoside Diphosphate Sugarsdecarboxylasesdehydratasesdehydrogenasesnatural productssugar nucleotides

Identifiers

PMID26289554
PMCPMC4598305

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.