Evidence map›Paper›PMID 22220568›Full record

ArticleThe Biochemical journal2012

Catalytic residues and a predicted structure of tetrahydrobiopterin-dependent alkylglycerol mono-oxygenase.

Katrin Watschinger, Julian E Fuchs, Vladimir Yarov-Yarovoy, Markus A Keller, Georg Golderer, Albin Hermetter, Gabriele Werner-Felmayer, Nicolas Hulo, Ernst R Werner

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Tetrahydrobiopterin and alkylglycerol monooxygenase substantially alter the murine macrophage lipidome.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Review
  11. 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

9 authors at 4 institutions in 2 countries.

Katrin WatschingerDivision of Biological Chemistry, Biocenter, Innsbruck Medical University, Fritz-Pregl-Strasse 3/VI, A-6020 Innsbruck, Austria.
Julian E Fuchs
Vladimir Yarov-Yarovoy
Markus A Keller
Georg Golderer
Albin Hermetter
Gabriele Werner-Felmayer
Nicolas Hulo
Ernst R Werner
Innsbruck Medical University · ATGraz University of Technology · ATSIB Swiss Institute of Bioinformatics · CHUniversität Innsbruck · AT

Funding

Austrian Science Fund FWF P 22406
6 · The paper itself

Abstract

Alkylglycerol mono-oxygenase (EC 1.14.16.5) forms a third, distinct, class among tetrahydrobiopterin-dependent enzymes in addition to aromatic amino acid hydroxylases and nitric oxide synthases. Its protein sequence contains the fatty acid hydroxylase motif, a signature indicative of a di-iron centre, which contains eight conserved histidine residues. Membrane enzymes containing this motif, including alkylglycerol mono-oxygenase, are especially labile and so far have not been purified to homogeneity in active form. To obtain a first insight into structure-function relationships of this enzyme, we performed site-directed mutagenesis of 26 selected amino acid residues and expressed wild-type and mutant proteins containing a C-terminal Myc tag together with fatty aldehyde dehydrogenase in Chinese-hamster ovary cells. Among all of the acidic residues within the eight-histidine motif, only mutation of Glu137 to alanine led to an 18-fold increase in the Michaelis-Menten constant for tetrahydrobiopterin, suggesting a role in tetrahydrobiopterin interaction. A ninth additional histidine residue essential for activity was also identified. Nine membrane domains were predicted by four programs: ESKW, TMHMM, MEMSAT and Phobius. Prediction of a part of the structure using the Rosetta membrane ab initio method led to a plausible suggestion for a structure of the catalytic site of alkylglycerol mono-oxygenase.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsBiopterinsCatalytic DomainCHO CellsComputer SimulationConsensus SequenceCricetinaeHumansIronKineticsMixed Function OxygenasesModels, MolecularMutagenesis, Site-DirectedProtein BindingBiopterinsglyceryl-ether monooxygenaseIronMixed Function OxygenasesRecombinant Proteinssapropterin

Identifiers

PMID22220568
PMCPMC3304488
OpenAlexW2040832737

What OpenQuestion holds

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LicenceCC BY-NC
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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.