Evidence map›Paper›PMID 18156253›Full record

ArticleJournal of bacteriology2008

Glycerate 2-kinase of Thermotoga maritima and genomic reconstruction of related metabolic pathways.

Chen Yang, Dmitry A Rodionov, Irina A Rodionova, Xiaoqing Li, Andrei L Osterman

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

20 citing papers in PubMed, 33 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

5 authors at 3 institutions in 3 countries.

Chen YangBurnham Institute for Medical Research, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
Dmitry A Rodionov
Irina A Rodionova
Xiaoqing Li
Andrei L Osterman
Institute for Medical Research · USCenter for Excellence in Molecular Plant Sciences · CNSanford Burnham Prebys Medical Discovery Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of a novel glycerate-2-kinase (GK-II) family were tentatively identified in a broad range of species, including eukaryotes and archaea and many bacteria that lack a canonical enzyme of the GarK (GK-I) family. The recently reported three-dimensional structure of GK-II from Thermotoga maritima (TM1585; PDB code 2b8n) revealed a new fold distinct from other known kinase families. Here, we verified the enzymatic activity of TM1585, assessed its kinetic characteristics, and used directed mutagenesis to confirm the essential role of the two active-site residues Lys-47 and Arg-325. The main objective of this study was to apply comparative genomics for the reconstruction of metabolic pathways associated with GK-II in all bacteria and, in particular, in T. maritima. Comparative analyses of approximately 400 bacterial genomes revealed a remarkable variety of pathways that lead to GK-II-driven utilization of glycerate via a glycolysis/gluconeogenesis route. In the case of T. maritima, a three-step serine degradation pathway was inferred based on the tentative identification of two additional enzymes, serine-pyruvate aminotransferase and hydroxypyruvate reductase (TM1400 and TM1401, respectively), that convert serine to glycerate via hydroxypyruvate. Both enzymatic activities were experimentally verified, and the entire pathway was validated by its in vitro reconstitution.

Indexed as

Genome, BacterialBacterial ProteinsComputational BiologyGenomicsGlyceric AcidsHydroxypyruvate ReductaseModels, BiologicalMutagenesis, Site-DirectedPhosphorylationPhosphotransferases (Alcohol Group Acceptor)PyruvatesRecombinant Fusion ProteinsRegulonSerineThermotoga maritimaTransaminasesBacterial Proteinsglycerate kinaseglyceric acidGlyceric AcidsHydroxypyruvate Reductasehydroxypyruvic acidPhosphotransferases (Alcohol Group Acceptor)PyruvatesRecombinant Fusion ProteinsSerineserine-pyruvate aminotransferaseTransaminases

Identifiers

PMID18156253
PMCPMC2258669
OpenAlexW2106891473

What OpenQuestion holds

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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.