Kinetická analýza a strukturní korelace reakce cytokinindehydrogenasy

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F05%3A00001818" target="_blank" >RIV/61989592:15310/05:00001818 - 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

Kinetic analysis and structural correlations of the reaction of cytokinin dehydrogenase (EC. 1.5.99.12)

Popis výsledku v původním jazyce

Cytokinin dehydrogenase (CKX) is a flavoprotein that cleaves cytokinins to adenine and corresponding side-chain aldehyde using a quinone-type electron acceptor. Reactions of maize CKX with five different substrates were studied using the Stopped-flow monitoring of the reductive half-reaction revealed formation of a binary ES complex between the formed cytokinin imine and the reduced enzyme. KD values for cytokinin binding range from <2 ?M for isopentenyladenine to 66 ?M for kinetin and reasonably correspond to respective Km values. Reduction rate was high for isoprenoid cytokinins that showed specific formation of a charge transfer complex with the enzyme, but very low for other cytokinins. The ES complex decays to form a free imine-product which accumulates in the reaction mixture and only slowly hydrolyzes to adenine and the corresponding aldehyde. The imine products were identified using Q-TOF MS/MS. Mixing of the substrate-reduced enzyme with Cu2+/imidazole as an electron acceptor,

Název v anglickém jazyce

Kinetic analysis and structural correlations of the reaction of cytokinin dehydrogenase (EC. 1.5.99.12)

Popis výsledku anglicky

Cytokinin dehydrogenase (CKX) is a flavoprotein that cleaves cytokinins to adenine and corresponding side-chain aldehyde using a quinone-type electron acceptor. Reactions of maize CKX with five different substrates were studied using the Stopped-flow monitoring of the reductive half-reaction revealed formation of a binary ES complex between the formed cytokinin imine and the reduced enzyme. KD values for cytokinin binding range from <2 ?M for isopentenyladenine to 66 ?M for kinetin and reasonably correspond to respective Km values. Reduction rate was high for isoprenoid cytokinins that showed specific formation of a charge transfer complex with the enzyme, but very low for other cytokinins. The ES complex decays to form a free imine-product which accumulates in the reaction mixture and only slowly hydrolyzes to adenine and the corresponding aldehyde. The imine products were identified using Q-TOF MS/MS. Mixing of the substrate-reduced enzyme with Cu2+/imidazole as an electron acceptor,

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

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

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

Název periodika

Biologia Plantarum

ISSN

0006-3134

e-ISSN

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Svazek periodika

49

Číslo periodika v rámci svazku

S1

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

1

Strana od-do

"S3"

Kód UT WoS článku

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EID výsledku v databázi Scopus

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