Biochemie a fyziologické funkce cytokinindehydrogenasy v rostlinách

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002096" target="_blank" >RIV/61989592:15310/04:00002096 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Biochemistry and physiological functions of cytokinin dehydrogenase in plants

Popis výsledku v původním jazyce

Degradation of growth hormones cytokinins in plants is controlled by flavoprotein cytokinin dehydrogenase (EC 1.5.99.12)1. This enzyme is encoded in individual species by multiple genes that show mutual evolutionary relations. Best studied gene family ofArabidopsis thaliana contains seven genes that appear to have different cellular and tissue targeting, thus achieving distinct functions during the development 1,2. The enzyme is a typical flavoprotein with covalently bound FAD in the catalytic centre that is buried in the hydrophobic pocket of the protein. Results of site-directed mutagenesis reveal C-terminus as an important domain for functional conformation of the enzyme. The cytokinin cleavage proceeds by #concerted covalent catalysis# via a ternary complex involving covalently bound FAD cofactor and a quinonic electron acceptor3. The enzyme is capable of using DCPIP and some p-quinones as electron acceptors, while oxygen is almost ineffective. Natural electron acceptor of the enz

Název v anglickém jazyce

Biochemistry and physiological functions of cytokinin dehydrogenase in plants

Popis výsledku anglicky

Degradation of growth hormones cytokinins in plants is controlled by flavoprotein cytokinin dehydrogenase (EC 1.5.99.12)1. This enzyme is encoded in individual species by multiple genes that show mutual evolutionary relations. Best studied gene family ofArabidopsis thaliana contains seven genes that appear to have different cellular and tissue targeting, thus achieving distinct functions during the development 1,2. The enzyme is a typical flavoprotein with covalently bound FAD in the catalytic centre that is buried in the hydrophobic pocket of the protein. Results of site-directed mutagenesis reveal C-terminus as an important domain for functional conformation of the enzyme. The cytokinin cleavage proceeds by #concerted covalent catalysis# via a ternary complex involving covalently bound FAD cofactor and a quinonic electron acceptor3. The enzyme is capable of using DCPIP and some p-quinones as electron acceptors, while oxygen is almost ineffective. Natural electron acceptor of the enz

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA522%2F03%2F0979" target="_blank" >GA522/03/0979: Organizace genů cytokinin dehydrogenázy v obilovinách a mechanismus katalytické reakce odbourávání cytokininů</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název periodika

Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica

ISSN

0232-0061

e-ISSN

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Svazek periodika

43

Číslo periodika v rámci svazku

S

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

275

Strana od-do

23

Kód UT WoS článku

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EID výsledku v databázi Scopus

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