Plant aminoaldehyde dehydrogenases oxidize a wide range of nitrogenous heterocyclic aldehydes

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F12%3A33142673" target="_blank" >RIV/61989592:15310/12:33142673 - isvavai.cz</a>

Alternative codes found

RIV/00216224:14740/12:00057220

Result on the web

<a href="http://dx.doi.org/10.1007/s00726-011-1174-x" target="_blank" >http://dx.doi.org/10.1007/s00726-011-1174-x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00726-011-1174-x" target="_blank" >10.1007/s00726-011-1174-x</a>

Result language

angličtina

Original language name

Plant aminoaldehyde dehydrogenases oxidize a wide range of nitrogenous heterocyclic aldehydes

Original language description

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 omega-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 theirsubstrate 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

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

2012

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

43

Issue of the periodical within the volume

3

Country of publishing house

AT - AUSTRIA

Number of pages

14

Pages from-to

1189-1202

UT code for WoS article

000307536100016

EID of the result in the Scopus database

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