Evidence map›Paper›PMID 23408433›Full record

ArticleThe Journal of biological chemistry2013

Plant ALDH10 family: identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate.

David Kopečny, Radka Končitíková, Martina Tylichová, Armelle Vigouroux, Hana Moskalíková, Miroslav Soural, Marek Šebela, Solange Moréra

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
1.9field-weighted citation impact, top 14% 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, 45 citations in OpenAlex.

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  19. Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  20. 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

8 authors at 3 institutions in 2 countries.

David KopečnyDepartment of Protein Biochemistry and Proteomics, Centre of the Region Haná for Biotechnological and Agricultural Research, Olomouc, Czech Republic. kopecny_david@yahoo.co.uk
Radka Končitíková
Martina Tylichová
Armelle Vigouroux
Hana Moskalíková
Miroslav Soural
Marek Šebela
Solange Moréra
Palacký University Olomouc · CZCentre National de la Recherche Scientifique · FRCentre of the Region Haná for Biotechnical and Agricultural Research · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant ALDH10 family members are aminoaldehyde dehydrogenases (AMADHs), which oxidize ω-aminoaldehydes to the corresponding acids. They have been linked to polyamine catabolism, osmoprotection, secondary metabolism (fragrance), and carnitine biosynthesis. Plants commonly contain two AMADH isoenzymes. We previously studied the substrate specificity of two AMADH isoforms from peas (PsAMADHs). Here, two isoenzymes from tomato (Solanum lycopersicum), SlAMADHs, and three AMADHs from maize (Zea mays), ZmAMADHs, were kinetically investigated to obtain further clues to the catalytic mechanism and the substrate specificity. We also solved the high resolution crystal structures of SlAMADH1 and ZmAMADH1a because these enzymes stand out from the others regarding their activity. From the structural and kinetic analysis, we can state that five residues at positions 163, 288, 289, 444, and 454 (PsAMADHs numbering) can, directly or not, significantly modulate AMADH substrate specificity. In the SlAMADH1 structure, a PEG aldehyde derived from the precipitant forms a thiohemiacetal intermediate, never observed so far. Its absence in the SlAMADH1-E260A structure suggests that Glu-260 can activate the catalytic cysteine as a nucleophile. We show that the five AMADHs studied here are capable of oxidizing 3-dimethylsulfoniopropionaldehyde to the cryo- and osmoprotectant 3-dimethylsulfoniopropionate. For the first time, we also show that 3-acetamidopropionaldehyde, the third aminoaldehyde besides 3-aminopropionaldehyde and 4-aminobutyraldehyde, is generally oxidized by AMADHs, meaning that these enzymes are unique in metabolizing and detoxifying aldehyde products of polyamine degradation to nontoxic amino acids. Finally, gene expression profiles in maize indicate that AMADHs might be important for controlling ω-aminoaldehyde levels during early stages of the seed development.

Indexed as

Gene Expression Regulation, EnzymologicGene Expression Regulation, PlantAldehyde OxidoreductasesAldehydesCrystallography, X-RayKineticsModels, ChemicalMutagenesis, Site-DirectedNADPhylogenyPlant Physiological PhenomenaPlantsPolyethylene GlycolsProtein BindingSeedsSolanum lycopersicumAldehyde OxidoreductasesAldehydesNADPolyethylene Glycols

Identifiers

PMID23408433
PMCPMC3611018
OpenAlexW2061421971

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.