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

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Abstract

Plant aminoaldehyde dehydrogenases (AMADHs, EC 1.2.1.19) 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.

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Abbreviations

Ac-ABAL:

4-Acetamidobutanal

Ac-APAL:

3-Acetamidopropanal

ALDH:

Aldehyde dehydrogenase

AMADH:

Aminoaldehyde dehydrogenase

APAL:

3-Aminopropanal

ABAL:

4-Aminobutanal

BAL:

Betaine aldehyde

BADH:

Betaine aldehyde dehydrogenase

GABA:

4-Aminobutyric acid

GBAL:

4-Guanidinobutanal

PsAMADH:

Aminoaldehyde dehydrogenase from pea (Pisum sativum)

TMABAL:

4-Trimethylaminobutanal

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Acknowledgments

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.

Author information

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, Marek Šebela, René Lenobel & David Kopečný

  2. Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic

    Gabriel Demo

  3. National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic

    Gabriel Demo

  4. Department of Chemical Biology, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University, Šlechtitelů 11, 783 71, Olomouc, Czech Republic

    Tomáš Pospíšil

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

    Miroslav Soural

  6. Institute of Molecular and Translational Medicine, Faculty of Medicine and Dentistry, Palacký University, Hněvotínská 5, Olomouc, CZ-779 00, Czech Republic

    Miroslav Soural

Authors
  1. Jan Frömmel
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  2. Marek Šebela
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  3. Gabriel Demo
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  4. René Lenobel
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  5. Tomáš Pospíšil
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  6. Miroslav Soural
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  7. David Kopečný
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Corresponding authors

Correspondence to Marek Šebela or David Kopečný.

Additional information

Abbreviations for names of all new synthetic N-acyl-ω-aminoaldehydes (15 compounds) are completely elucidated in the supplementary file 1 (Met stands for methyl, Propi for propionyl, Butyr for butyryl, Valer for valeryl and Adip for adipoyl).

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Frömmel, J., Šebela, M., Demo, G. et al. N-acyl-ω-aminoaldehydes are efficient substrates of plant aminoaldehyde dehydrogenases. Amino Acids 47, 175–187 (2015). https://doi.org/10.1007/s00726-014-1853-5

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