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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F15%3A33156900" target="_blank" >RIV/61989592:15310/15:33156900 - isvavai.cz</a>

Alternative codes found

RIV/00216224:14740/15:00082146 RIV/61989592:15110/15:33156900

Result on the web

<a href="http://link.springer.com/article/10.1007%2Fs00726-014-1853-5" target="_blank" >http://link.springer.com/article/10.1007%2Fs00726-014-1853-5</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00726-014-1853-5" target="_blank" >10.1007/s00726-014-1853-5</a>

Result language

angličtina

Original language name

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

Original language description

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 omega-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 Angstroem x 14 Angstroem). 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 Km 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.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2015

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Amino Acids

ISSN

0939-4451

e-ISSN

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Volume of the periodical

47

Issue of the periodical within the volume

1

Country of publishing house

AT - AUSTRIA

Number of pages

13

Pages from-to

"175-187"

UT code for WoS article

000347248500016

EID of the result in the Scopus database

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