Biochemie cytokinindehydrogenasy

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002099" target="_blank" >RIV/61989592:15310/04:00002099 - 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 of cytokinin dehydrogenase.

Popis výsledku v původním jazyce

Degradation of cytokinins in plants is controlled by flavoprotein cytokinin dehydrogenase (EC 1.5.99.12). Kinetic measurements and stopped-flow spectrophotometry on a recombinant enzyme from maize (ZmCKX1) revealed that the cleavage of cytokinin substrates proceeds via ternary complex involving FAD cofactor and a quinonic electron acceptor (2,3-dimethoxy-5-methyl-1,4-benzoquinone as a model compound). Results of site-directed mutagenesis and structural homology modeling disclosed C-terminus of the protein as an important domain for functional conformation of the enzyme, with the covalently bound FAD cofactor being buried in a hydrophobic pocket. Functional electron acceptors of ZmCKX1 were generated in vitro from acetosyringone and some catechols and flavonoids by conversion either with peroxidase/hydrogen peroxide system or mushroom tyrosinase (a commercial substitute for plant catechol oxidase/laccase). Histochemical localizations in maize kernel showed co-staining of cytokinin dehyd

Název v anglickém jazyce

Biochemistry of cytokinin dehydrogenase.

Popis výsledku anglicky

Degradation of cytokinins in plants is controlled by flavoprotein cytokinin dehydrogenase (EC 1.5.99.12). Kinetic measurements and stopped-flow spectrophotometry on a recombinant enzyme from maize (ZmCKX1) revealed that the cleavage of cytokinin substrates proceeds via ternary complex involving FAD cofactor and a quinonic electron acceptor (2,3-dimethoxy-5-methyl-1,4-benzoquinone as a model compound). Results of site-directed mutagenesis and structural homology modeling disclosed C-terminus of the protein as an important domain for functional conformation of the enzyme, with the covalently bound FAD cofactor being buried in a hydrophobic pocket. Functional electron acceptors of ZmCKX1 were generated in vitro from acetosyringone and some catechols and flavonoids by conversion either with peroxidase/hydrogen peroxide system or mushroom tyrosinase (a commercial substitute for plant catechol oxidase/laccase). Histochemical localizations in maize kernel showed co-staining of cytokinin dehyd

Druh

D - Stať ve sborníku

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 statě ve sborníku

Conference Handbook, 18th International Conference on Plant Growth Substances

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

144

Strana od-do

55

Název nakladatele

IPGSA

Místo vydání

Canberra, Australia

Místo konání akce

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Datum konání akce

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Typ akce podle státní příslušnosti

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Kód UT WoS článku

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