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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61389030:_____/15:00446876

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Biochemical Journal

ISSN

0264-6021

e-ISSN

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Svazek periodika

468

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

15

Strana od-do

109-123

Kód UT WoS článku

000353895700010

EID výsledku v databázi Scopus

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