Cytokinin oxidase (or cytokinin dehydrogenase?) from wheat: Purification, characterization and evidence for dehydrogenase mechanism of the enzyme reaction.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F99%3A00000767" target="_blank" >RIV/61989592:15310/99:00000767 - 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

Cytokinin oxidase (or cytokinin dehydrogenase?) from wheat: Purification, characterization and evidence for dehydrogenase mechanism of the enzyme reaction.

Popis výsledku v původním jazyce

The key enzyme in the degradation of plant hormones cytokinins, generally termed cytokinin oxidase, was purified to homogeneity from swollen wheat grains (Triticum aestivum) by a multistep procedure including low pressure chromatography, preparative electrophoresis and extensive FPLC separations resulting in a purification degree over 3,300-fold. New techniques were developed for the enzyme activity assay and staining on native electrophoretic gels to confirm the identity of the protein. The enzyme wasobtained with the highest specific activity ever reported, 44 nkat/mg. Purified enzyme is a monomeric flavoprotein of 39 kDa. The enzyme catalyzes the cleavage of N6-unsaturated isoprenoid side chain of cytokinins, preferably with a hydrophilic group inposition 2 of the purine ring, while the compounds with aromatic side chains on N6 are inhibitors. Contrary to the generally accepted view, it was found that oxygen is not required for the catalytic reaction and hydrogen peroxide is not p

Název v anglickém jazyce

Cytokinin oxidase (or cytokinin dehydrogenase?) from wheat: Purification, characterization and evidence for dehydrogenase mechanism of the enzyme reaction.

Popis výsledku anglicky

The key enzyme in the degradation of plant hormones cytokinins, generally termed cytokinin oxidase, was purified to homogeneity from swollen wheat grains (Triticum aestivum) by a multistep procedure including low pressure chromatography, preparative electrophoresis and extensive FPLC separations resulting in a purification degree over 3,300-fold. New techniques were developed for the enzyme activity assay and staining on native electrophoretic gels to confirm the identity of the protein. The enzyme wasobtained with the highest specific activity ever reported, 44 nkat/mg. Purified enzyme is a monomeric flavoprotein of 39 kDa. The enzyme catalyzes the cleavage of N6-unsaturated isoprenoid side chain of cytokinins, preferably with a hydrophilic group inposition 2 of the purine ring, while the compounds with aromatic side chains on N6 are inhibitors. Contrary to the generally accepted view, it was found that oxygen is not required for the catalytic reaction and hydrogen peroxide is not p

Druh

C - Kapitola v odborné knize

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

1999

Kód důvěrnosti údajů

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

Název knihy nebo sborníku

International Symposium on Auxins and cytokinins in plant development, Book of Abstracts (Biol. Plantarum, Vol. 42)

ISBN

0006-3134

Počet stran výsledku

122

Strana od-do

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Počet stran knihy

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Název nakladatele

Česká akademie věd

Místo vydání

Praha

Kód UT WoS kapitoly

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