Plant ALDH10 family: identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F13%3A33147799" target="_blank" >RIV/61989592:15310/13:33147799 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.jbc.org/content/288/13/9491" target="_blank" >http://www.jbc.org/content/288/13/9491</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M112.443952" target="_blank" >10.1074/jbc.M112.443952</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Plant ALDH10 family: identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate

Popis výsledku v původním jazyce

Plant ALDH10 family members are aminoaldehyde dehydrogenases (AMADHs), which oxidize omega-aminoaldehydes to the corresponding acids. They have been linked to polyamine catabolism, osmoprotection, secondary metabolism (fragrance), and carnitine biosynthesis. Plants commonly contain two AMADH isoenzymes. We previously studied the substrate specificity of two AMADH isoforms from peas (PsAMADHs). Here, two isoenzymes from tomato (Solanum lycopersicum), SlAMADHs, and three AMADHs from maize (Zea mays), ZmAMADHs, were kinetically investigated to obtain further clues to the catalytic mechanism and the substrate specificity. We also solved the high resolution crystal structures of SlAMADH1 and ZmAMADH1a because these enzymes stand out from the others regarding their activity. From the structural and kinetic analysis, we can state that five residues at positions 163, 288, 289, 444, and 454 (PsAMADHs numbering) can, directly or not, significantly modulate AMADH substrate specificity. In the SlA

Název v anglickém jazyce

Plant ALDH10 family: identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate

Popis výsledku anglicky

Plant ALDH10 family members are aminoaldehyde dehydrogenases (AMADHs), which oxidize omega-aminoaldehydes to the corresponding acids. They have been linked to polyamine catabolism, osmoprotection, secondary metabolism (fragrance), and carnitine biosynthesis. Plants commonly contain two AMADH isoenzymes. We previously studied the substrate specificity of two AMADH isoforms from peas (PsAMADHs). Here, two isoenzymes from tomato (Solanum lycopersicum), SlAMADHs, and three AMADHs from maize (Zea mays), ZmAMADHs, were kinetically investigated to obtain further clues to the catalytic mechanism and the substrate specificity. We also solved the high resolution crystal structures of SlAMADH1 and ZmAMADH1a because these enzymes stand out from the others regarding their activity. From the structural and kinetic analysis, we can state that five residues at positions 163, 288, 289, 444, and 454 (PsAMADHs numbering) can, directly or not, significantly modulate AMADH substrate specificity. In the SlA

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

2013

Kód důvěrnosti údajů

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

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Svazek periodika

288

Číslo periodika v rámci svazku

13

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

17

Strana od-do

9491-9507

Kód UT WoS článku

000316862200065

EID výsledku v databázi Scopus

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