Role and structural characterization of plant aldehyde dehydrogenases from family 2 and family 7

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F15%3A33156915" target="_blank" >RIV/61989592:15310/15:33156915 - isvavai.cz</a>

Alternative codes found

RIV/61389030:_____/15:00446876

Result on the web

<a href="http://dx.doi.org/10.1042/BJ20150009" target="_blank" >http://dx.doi.org/10.1042/BJ20150009</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1042/BJ20150009" target="_blank" >10.1042/BJ20150009</a>

Result language

angličtina

Original language name

Role and structural characterization of plant aldehyde dehydrogenases from family 2 and family 7

Original language description

Aldehyde dehydrogenases (ALDHs) are responsible for oxidation of biogenic aldehyde intermediates as well as for cell detoxification of aldehydes generated during lipid peroxidation. So far, 13 ALDH families have been described in plants. In the present study, we provide a detailed biochemical characterization of plant ALDH2 and ALDH7 families byanalysing maize and pea ALDH7 (ZmALDH7 and PsALDH7) and four maize cytosolic ALDH(cALDH)2 isoforms RF2C, RF2D, RF2E and RF2F [the first maize ALDH2 was discovered as a fertility restorer (RF2A)]. We report the crystal structures of ZmALDH7, RF2C and RF2F at high resolution. The ZmALDH7 structure shows that the three conserved residues Glu120, Arg300 and Thr302 in the ALDH7 family are located in the substrate-binding site and are specific to this family. Our kinetic analysis demonstrates that alpha-aminoadipic semialdehyde, a lysine catabolism intermediate, is the preferred substrate for plant ALDH7. In contrast, aromatic aldehydes including benz

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

Biochemical Journal

ISSN

0264-6021

e-ISSN

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Volume of the periodical

468

Issue of the periodical within the volume

1

Country of publishing house

GB - UNITED KINGDOM

Number of pages

15

Pages from-to

109-123

UT code for WoS article

000353895700010

EID of the result in the Scopus database

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