Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F11%3A10223645" target="_blank" >RIV/61989592:15310/11:10223645 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1111/j.1742-4658.2011.08239.x" target="_blank" >http://dx.doi.org/10.1111/j.1742-4658.2011.08239.x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/j.1742-4658.2011.08239.x" target="_blank" >10.1111/j.1742-4658.2011.08239.x</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases

Popis výsledku v původním jazyce

The characterization of the PsAMADH2 proteins, altered here by site-directed mutagenesis, suggests that the D110 and D113 residues at the entrance to the substrate channel are required for high-affinity binding of omega-aminoaldehydes to PsAMADH2 and forenzyme activity, whereas N162, near catalytic C294, contributes mainly to the enzyme's catalytic rate. Inside the substrate cavity, W170 and Y163, and, to a certain extent, L166 and M167 probably preserve the optimal overall geometry of the substrate channel that allows for the appropriate orientation of the substrate. Unconserved W288 appears to affect the affinity of the enzyme for the substrate amino group through control of the substrate channel diameter without affecting the reaction rate. Therefore, W288 may be a key determinant of the differences in substrate specificity found among plant AMADH isoforms when they interact with naturally occurring substrates such as 3-aminopropionaldehyde and 4-aminobutyraldehyde.

Název v anglickém jazyce

Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases

Popis výsledku anglicky

The characterization of the PsAMADH2 proteins, altered here by site-directed mutagenesis, suggests that the D110 and D113 residues at the entrance to the substrate channel are required for high-affinity binding of omega-aminoaldehydes to PsAMADH2 and forenzyme activity, whereas N162, near catalytic C294, contributes mainly to the enzyme's catalytic rate. Inside the substrate cavity, W170 and Y163, and, to a certain extent, L166 and M167 probably preserve the optimal overall geometry of the substrate channel that allows for the appropriate orientation of the substrate. Unconserved W288 appears to affect the affinity of the enzyme for the substrate amino group through control of the substrate channel diameter without affecting the reaction rate. Therefore, W288 may be a key determinant of the differences in substrate specificity found among plant AMADH isoforms when they interact with naturally occurring substrates such as 3-aminopropionaldehyde and 4-aminobutyraldehyde.

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)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

F E B S Journal

ISSN

1742-464X

e-ISSN

—

Svazek periodika

278

Číslo periodika v rámci svazku

17

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

10

Strana od-do

3130-3139

Kód UT WoS článku

000294025800016

EID výsledku v databázi Scopus

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