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Description
| - V článku je popsána biochemie a fyziologické funkce cytokinindehydrogenasy v rostlinách. (cs)
- 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 of Arabidopsis 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 enzyme is not yet k
- 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 of Arabidopsis 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 enzyme is not yet k (en)
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Title
| - Biochemie a fyziologické funkce cytokinindehydrogenasy v rostlinách (cs)
- Biochemistry and physiological functions of cytokinin dehydrogenase in plants
- Biochemistry and physiological functions of cytokinin dehydrogenase in plants (en)
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skos:prefLabel
| - Biochemie a fyziologické funkce cytokinindehydrogenasy v rostlinách (cs)
- Biochemistry and physiological functions of cytokinin dehydrogenase in plants
- Biochemistry and physiological functions of cytokinin dehydrogenase in plants (en)
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skos:notation
| - RIV/61989592:15310/04:00002096!RIV/2005/GA0/153105/N
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http://linked.open.../vavai/riv/strany
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
| - P(GA522/03/0979), Z(MSM 153100008)
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/61989592:15310/04:00002096
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - cytokinin oxidase/dehydrogenase;cytokinin metabolism (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/nazevZdroje
| - Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...v/svazekPeriodika
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http://linked.open...iv/tvurceVysledku
| - Drábek, Jiří
- Popelková, Hana
- Frébort, Ivo
- Frébortová, Jitka
- Galuszka, Petr
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http://linked.open...n/vavai/riv/zamer
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issn
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number of pages
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http://localhost/t...ganizacniJednotka
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