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Plant aminoaldehyde dehydrogenases oxidize a wide range of nitrogenous heterocyclic aldehydes

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Abstract

The metabolic degradation of aldehydes is catalyzed by oxidoreductases from which aldehyde dehydrogenases (EC 1.2.1) comprise nonspecific or substrate-specific enzymes. The latter subset is represented, e.g., by NAD+-dependent aminoaldehyde dehydrogenases (AMADHs; EC 1.2.1.19) oxidizing a group of naturally occurring ω-aminoaldehydes including polyamine oxidation products. Recombinant isoenzymes from pea (PsAMADH1 and 2) and tomato (LeAMADH1 and 2) were subjected to kinetic measurements with synthetic aldehydes containing a nitrogenous heterocycle such as pyridinecarbaldehydes and their halogenated derivatives, (pyridinylmethylamino)-aldehydes, pyridinyl propanals and aldehydes derived from purine, 7-deazapurine and pyrimidine to characterize their substrate specificity and significance of the resulting data for in vivo reactions. The enzymatic production of the corresponding carboxylic acids was analyzed by liquid chromatography coupled to electrospray ionization mass spectrometry. Although the studied AMADHs are largely homologous and supposed to have a very similar active site architecture, significant differences were observed. LeAMADH1 displayed the broadest specificity oxidizing almost all compounds followed by PsAMADH2 and 1. In contrast, LeAMADH2 accepted only a few compounds as substrates. Pyridinyl propanals were converted by all isoenzymes, usually better than pyridinecarbaldehydes and aldehydes with fused rings. The K m values for the best substrates were in the range of 10−5–10−4 M. Nevertheless, the catalytic efficiency values (V max/K m) reached only a very small fraction of that with 3-aminopropanal (except for LeAMADH1 activity with two pyridine-derived compounds). Docking experiments using the crystal structure of PsAMADH2 were involved to discuss differences in results with position isomers or alkyl chain homologs.

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Abbreviations

AMADH:

Aminoaldehyde dehydrogenase

AEAL:

2-Aminoethanal

ABAL:

4-Aminobutanal

ALDH:

Aldehyde dehydrogenase

APAL:

3-Aminopropanal

BADH:

Betaine aldehyde dehydrogenase

LeAMADH:

Tomato (Lycopersicon esculentum) aminoaldehyde dehydrogenase

LC–MS:

Liquid chromatography coupled to mass spectrometry

PsAMADH:

Pea (Pisum sativum) aminoaldehyde dehydrogenase

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Acknowledgments

This work was supported by OP RD&I grant no. ED0007/01/01 (Centre of the Region Haná for Biotechnological and Agricultural Research) and grant no. MSM0021622413 from the Ministry of Education, Youth and Sports, Czech Republic, plus grant no. 522/08/0555 from the Czech Science Foundation. We would also like to thank Hana Moskalíková, a former student of the Department of Biochemistry, Faculty of Science, Palacký University, for her valuable contribution to initial experiments.

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The authors declare no conflict of interest.

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Authors and Affiliations

  1. Department of Protein Biochemistry and Proteomics, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University, Šlechtitelů 11, 783 71, Olomouc, Czech Republic

    Jan Frömmel, Martina Tylichová, David Kopečný & Marek Šebela

  2. Department of Organic Chemistry, Faculty of Science, Palacký University, 17. listopadu 12, 771 46, Olomouc, Czech Republic

    Miroslav Soural

  3. Central European Institute of Technology and Department of Biochemistry, Faculty of Science, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic

    Gabriel Demo & Michaela Wimmerová

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  1. Jan Frömmel
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Correspondence to Miroslav Soural or Marek Šebela.

Additional information

Chemical names of all synthetic aldehyde compounds are abbreviated by acronyms (elucidated directly in the text) ending with a suffix AL.

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Frömmel, J., Soural, M., Tylichová, M. et al. Plant aminoaldehyde dehydrogenases oxidize a wide range of nitrogenous heterocyclic aldehydes. Amino Acids 43, 1189–1202 (2012). https://doi.org/10.1007/s00726-011-1174-x

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