Evidence map›Paper›PMID 17425781›Full record

ArticleBMC biochemistry2007

A novel bifunctional N-acetylglutamate synthase-kinase from Xanthomonas campestris that is closely related to mammalian N-acetylglutamate synthase.

Qiuhao Qu, Hiroki Morizono, Dashuang Shi, Mendel Tuchman, Ljubica Caldovic

Open access · hybridAbstract read
In one paragraph

Article in BMC biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 29 citations in OpenAlex.

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  5. The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms.International journal of molecular sciences · 2015
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  16. N-acetylglutamate synthase: structure, function and defects.Molecular genetics and metabolism · 2010
    Review
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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 1 country.

Qiuhao QuChildren's Research Institute, Children's National Medical Center, The George Washington University, Washington, DC 20010, USA. QQu@coh.org <QQu@coh.org>
Hiroki Morizono
Dashuang Shi
Mendel Tuchman
Ljubica Caldovic
Children's National · USCity Of Hope National Medical Center · USGeorge Washington University · US

Funding

N-acetylglutamate Synthase: Structure, Function & DefectsR01DK064913 · NIDDK · CHILDREN'S RESEARCH INSTITUTE · PI CALDOVIC, LJUBICA MORIZONO · 2003 to 2017
$4.9M
NIDDK NIH HHS R01 DK064913
6 · The paper itself

Abstract

backgroundIn microorganisms and plants, the first two reactions of arginine biosynthesis are catalyzed by N-acetylglutamate synthase (NAGS) and N-acetylglutamate kinase (NAGK). In mammals, NAGS produces an essential activator of carbamylphosphate synthetase I, the first enzyme of the urea cycle, and no functional NAGK homolog has been found. Unlike the other urea cycle enzymes, whose bacterial counterparts could be readily identified by their sequence conservation with arginine biosynthetic enzymes, mammalian NAGS gene was very divergent, making it the last urea cycle gene to be discovered. Limited sequence similarity between E. coli NAGS and fungal NAGK suggests that bacterial and eukaryotic NAGS, and fungal NAGK arose from the fusion of genes encoding an ancestral NAGK (argB) and an acetyltransferase. However, mammalian NAGS no longer retains any NAGK catalytic activity.

resultsWe identified a novel bifunctional N-acetylglutamate synthase and kinase (NAGS-K) in the Xanthomonadales order of gamma-proteobacteria that appears to resemble this postulated primordial fusion protein. Phylogenetic analysis indicated that xanthomonad NAGS-K is more closely related to mammalian NAGS than to other bacterial NAGS. We cloned the NAGS-K gene from Xanthomonas campestis, and characterized the recombinant NAGS-K protein. Mammalian NAGS and its bacterial homolog have similar affinities for substrates acetyl coenzyme A and glutamate as well as for their allosteric regulator arginine.

conclusionThe close phylogenetic relationship and similar biochemical properties of xanthomonad NAGS-K and mammalian NAGS suggest that we have identified a close relative to the bacterial antecedent of mammalian NAGS and that the enzyme from X. campestris could become a good model for mammalian NAGS in structural, biochemical and biophysical studies.

Indexed as

Acetyl Coenzyme AAmino-Acid N-AcetyltransferaseAmino Acid SequenceAnimalsArginineCloning, MolecularConserved SequenceHumansHydrogen-Ion ConcentrationIsoenzymesMammalsMolecular Sequence DataPhosphotransferases (Carboxyl Group Acceptor)PhylogenyRecombinant ProteinsSequence AlignmentAcetyl Coenzyme Aacetylglutamate kinaseAmino-Acid N-AcetyltransferaseArginineIsoenzymesPhosphotransferases (Carboxyl Group Acceptor)Recombinant Proteins

Identifiers

PMID17425781
PMCPMC1865377
OpenAlexW2037662484

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.