Amino Acids

, Volume 47, Issue 1, pp 175–187 | Cite as

N-acyl-ω-aminoaldehydes are efficient substrates of plant aminoaldehyde dehydrogenases

  • Jan Frömmel
  • Marek Šebela
  • Gabriel Demo
  • René Lenobel
  • Tomáš Pospíšil
  • Miroslav Soural
  • David Kopečný
Original Article


Plant aminoaldehyde dehydrogenases (AMADHs, EC belong to the family 10 of aldehyde dehydrogenases and participate in the metabolism of compounds related to amino acids such as polyamines or osmoprotectants. Their broad specificity covers ω-aminoaldehydes, aliphatic and aromatic aldehydes as well as nitrogen-containing heterocyclic aldehydes. The substrate preference of plant AMADHs is determined by the presence of aspartic acid and aromatic residues in the substrate channel. In this work, 15 new N-acyl derivates of 3-aminopropanal (APAL) and 4-aminobutanal (ABAL) were synthesized and confirmed as substrates of two pea AMADH isoenzymes (PsAMADH 1 and 2). The compounds were designed considering the previously demonstrated conversion of N-acetyl derivatives as well as substrate channel dimensions (5–8 Å × 14 Å). The acyl chain length and its branching were found less significant for substrate properties than the length of the initial natural substrate. In general, APAL derivatives were found more efficient than the corresponding ABAL derivatives because of the prevailing higher conversion rates and lower K m values. Differences in enzymatic performance between the two isoenzymes corresponded in part to their preferences to APAL to ABAL. The higher PsAMADH2 affinity to substrates correlated with more frequent occurrence of an excess substrate inhibition. Molecular docking indicated the possible auxiliary role of Tyr163, Ser295 and Gln451 in binding of the new substrates. The only derivative carrying a free carboxyl group (N-adipoyl APAL) was surprisingly better substrate than ABAL in PsAMADH2 reaction indicating that also negatively charged aldehydes might be good substrates for ALDH10 family.


N-acylation Aminoaldehyde dehydrogenase Isoenzyme KF-celite NAD+ Substrate docking 







Aldehyde dehydrogenase


Aminoaldehyde dehydrogenase






Betaine aldehyde


Betaine aldehyde dehydrogenase


4-Aminobutyric acid




Aminoaldehyde dehydrogenase from pea (Pisum sativum)





This work was supported by Grant No. LO1204 from the Ministry of Education, Youth and Sports of the Czech Republic and Grant No. P501/11/1591 from the Czech Science Foundation. The authors thank for the access to computing and storage facilities owned by parties and projects contributing to the National Grid Infrastructure MetaCentrum provided under the program “Projects of Large Infrastructure for Research, Development, and Innovations” (LM2010005).

Conflict of interest

The authors declare no conflict of interest.

Supplementary material

726_2014_1853_MOESM1_ESM.doc (684 kb)
Supplementary material 1 (DOC 684 kb)
726_2014_1853_MOESM2_ESM.doc (46 kb)
Supplementary material 2 (DOC 46 kb)
726_2014_1853_MOESM3_ESM.pptx (236 kb)
Supplementary material 3 (PPTX 236 kb)


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Copyright information

© Springer-Verlag Wien 2014

Authors and Affiliations

  • Jan Frömmel
    • 1
  • Marek Šebela
    • 1
  • Gabriel Demo
    • 2
    • 3
  • René Lenobel
    • 1
  • Tomáš Pospíšil
    • 4
  • Miroslav Soural
    • 5
    • 6
  • David Kopečný
    • 1
  1. 1.Department of Protein Biochemistry and Proteomics, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of SciencePalacký UniversityOlomoucCzech Republic
  2. 2.Central European Institute of TechnologyMasaryk UniversityBrnoCzech Republic
  3. 3.National Centre for Biomolecular Research, Faculty of ScienceMasaryk UniversityBrnoCzech Republic
  4. 4.Department of Chemical Biology, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of SciencePalacký UniversityOlomoucCzech Republic
  5. 5.Department of Organic Chemistry, Faculty of SciencePalacký UniversityOlomoucCzech Republic
  6. 6.Institute of Molecular and Translational Medicine, Faculty of Medicine and DentistryPalacký UniversityOlomoucCzech Republic

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