Evidence map›Paper›PMID 19588076›Full record

ArticleCellular and molecular life sciences : CMLS2009

The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase.

Sam Kaitaniemi, Heli Elovaara, Kirsi Grön, Heidi Kidron, Janne Liukkonen, Tiina Salminen, Marko Salmi, Sirpa Jalkanen, Kati Elima

Open access · greenAbstract readComparative Study
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

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  13. Human copper-dependent amine oxidases.Archives of biochemistry and biophysics · 2014
    Review
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  18. A new crystal form of human vascular adhesion protein 1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
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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

9 authors at 5 institutions in 2 countries.

Sam KaitaniemiMediCity Research Laboratory, University of Turku, and National Institute for Health and Welfare, Tykistökatu 6, 20520 Turku, Finland.
Heli Elovaara
Kirsi Grön
Heidi Kidron
Janne Liukkonen
Tiina Salminen
Marko Salmi
Sirpa Jalkanen
Kati Elima
University of Turku · FIÅbo Akademi University · FINational Institutes of Health · USFinnish Institute for Health and Welfare · FITurku University Hospital · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Semicarbazide-sensitive amine oxidases (SSAOs) catalyze oxidative deamination of primary amines, but the true physiological function of these enzymes is still poorly understood. Here, we have studied the functional and structural characteristics of a human cell-surface SSAO, AOC2, which is homologous to the better characterized family member, AOC3. The preferred in vitro substrates of AOC2 were found to be 2-phenylethylamine, tryptamine and p-tyramine instead of methylamine and benzylamine, the favored substrates of AOC3. Molecular modeling suggested structural differences between AOC2 and AOC3, which provide AOC2 with the capability to use the larger monoamines as substrates. Even though AOC2 mRNA was expressed in many tissues, the only tissues with detectable AOC2-like enzyme activity were found in the eye. Characterization of AOC2 will help in evaluating the contribution of this enzyme to the pathological processes attributed to the SSAO activity and in designing specific inhibitors for the individual members of the SSAO family.

Indexed as

Amine Oxidase (Copper-Containing)Cell Adhesion MoleculesCloning, MolecularDimerizationEyeEye ProteinsHumansKineticsModels, MolecularMutagenesis, Site-DirectedOxidoreductases Acting on CH-NH Group DonorsPhenethylaminesProtein Structure, TertiaryRNA, MessengerSubstrate SpecificityTryptaminesAmine Oxidase (Copper-Containing)AOC2 protein, humanAOC3 protein, humanCell Adhesion MoleculesEye ProteinsOxidoreductases Acting on CH-NH Group DonorsphenethylaminePhenethylaminesRNA, MessengertryptamineTryptaminesTyramine

Identifiers

PMID19588076
PMCPMC11115939
OpenAlexW2094727479

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.