Tissue localization of cytokinin dehydrogenase in maize: Possible involvement of quinone species generated from plant phenolics by other enzymatic systems in the catalytic reaction

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F05%3A00001819" target="_blank" >RIV/61989592:15310/05:00001819 - isvavai.cz</a>

Alternative codes found

RIV/61389030:_____/05:00083396

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Tissue localization of cytokinin dehydrogenase in maize: Possible involvement of quinone species generated from plant phenolics by other enzymatic systems in the catalytic reaction

Original language description

The degradation of cytokinins in plants is controlled by the flavoprotein cytokinin dehydrogenase (EC 1.5.99.12). Cytokinin dehydrogenase from maize showed the ability to use oxidation products of guaiacol, 4-methylcatechol, acetosyringone and several other compounds as electron acceptors. These results led us to explore the cability for indirect production of suitable electron acceptors by different quinone-generating enzymes. The results reported here revealed that the electron acceptors may be generated in vivo from plant phenolics by other enzymatic systems such as peroxidase and tyrosinase/laccase/catechol oxidase. Histochemical localization of cytokinin dehydrogenase by activity staining and immunochemistry using optical and confocal microscopy showed that cytokinin dehydrogenase is most abundant in the aleurone layer of maize kernels and in phloem cells of the seedling shoots. Cytokinin dehydrogenase was confirmed to be present in the apoplast of cells. Co-staining of enzyme act

Czech name

Lokalizace cytokinindehydrogenasy v kukuřičných pletivech: úloha chinonových látek vzniklých z rostlinných fenolátů působením jiných enzymových systémů v katalytickém mechanismu

Czech description

Enzym cytokininoxidasa/dehydrogenasa katalyzuje degradaci rostlinných hormonů cytokininů. V této práci je prokázáno, že látky generované in vivo enzymovou oxidací fenolových látek (např. hydroxyderivátů k. benzoové a skořicové) mohou sloužit jako přirozené akceptory elektronů v katalyzované reakci. Byla rovněž provedena histochemická a imunohistochemická lokalizace enzymu v rostlinných pletivech. Enzym je lokalizován v apoplastu, výsledky naznačují jeho možné spolupůsobení s enzymem lakasou.

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

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

Publication year

2005

Confidentiality

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

Name of the periodical

Plant and Cell Physiology

ISSN

0032-0781

e-ISSN

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Volume of the periodical

46

Issue of the periodical within the volume

5

Country of publishing house

GB - UNITED KINGDOM

Number of pages

13

Pages from-to

716-728

UT code for WoS article

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EID of the result in the Scopus database

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