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rdf:type
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Description
| - Rostlinné enzymy účastnící se degradace nitroaromatických látek dosud nebyly podrobněji biochemicky charakterizovány. Ze suspensní kultury mydlice lékařské (Saponaria officinalis L.) jsme izolovali novou rostlinnou oxidoreduktázu, která se účastní degradace trinitrotoluenu (TNT). Tento enzym katalyzuje první krok redukce nitroskupin TNT za přítomnosti NAD(P)H za anaerobních podmínek. Enzym je monomerní, má molekulovou hmotnost 29 kDa a vyskytuje se ve dvou isoformách (pI 4,8 a 5,1). podle spektrální a kativační analýzy enzym obsahuje flavinmononukleotid jako prostetickou skupinu. Ze strukturálních vlastností lze usuzovat na evoluční příbuznost k oxofytodienoát reduktáze. Pořadí aminokyselin N-terminálního konce vykazuje homologii s rodinou OYE (E.C. 1.6.99.1). (cs)
- Plant enzymes participating in degradation of nitroaromatic compounds have not been biochemically characterized in details so far. From suspension culture of soapwort (Saponaria officinalis L.) we isolated a novel plant oxidoreductase involved in degradation of trinitrotoluene (TNT). The enzyme catalyses first steps of reduction of TNT nitro groups in the presence of NAD(P)H under anaerobic conditions. The enzyme is monomeric with molecular mass 29 kDa, its two isoforms have pI 4.8 and 5.1. According to the spectral and activation analysis the enzyme contains flavinmono-nucleotide as a prosthetic group. The structure properties suggest an evolutional relationship to oxophytodienoate reductase. The N-terminal amino acid sequence shows homology to family of Old Yellow Enzyme (E.C. 1.6.99.1).
- Plant enzymes participating in degradation of nitroaromatic compounds have not been biochemically characterized in details so far. From suspension culture of soapwort (Saponaria officinalis L.) we isolated a novel plant oxidoreductase involved in degradation of trinitrotoluene (TNT). The enzyme catalyses first steps of reduction of TNT nitro groups in the presence of NAD(P)H under anaerobic conditions. The enzyme is monomeric with molecular mass 29 kDa, its two isoforms have pI 4.8 and 5.1. According to the spectral and activation analysis the enzyme contains flavinmono-nucleotide as a prosthetic group. The structure properties suggest an evolutional relationship to oxophytodienoate reductase. The N-terminal amino acid sequence shows homology to family of Old Yellow Enzyme (E.C. 1.6.99.1). (en)
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Title
| - Soapwort oxidoreductase is involved in trinitrotoluene detoxification
- Soapwort oxidoreductase is involved in trinitrotoluene detoxification (en)
- Soapwort oxidoreductase is involved in trinitrotoluene detoxification (cs)
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skos:prefLabel
| - Soapwort oxidoreductase is involved in trinitrotoluene detoxification
- Soapwort oxidoreductase is involved in trinitrotoluene detoxification (en)
- Soapwort oxidoreductase is involved in trinitrotoluene detoxification (cs)
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skos:notation
| - RIV/61388963:_____/07:00305940!RIV08-AV0-61388963
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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(1P05ME730), P(1P05OC042), V, Z(AV0Z40550506), Z(AV0Z50380511)
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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/61388963:_____/07:00305940
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - flavoprotein; Old Yellow Enzyme; oxidoreductase (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
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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
| - Podlipná, Radka
- Vaněk, Tomáš
- Vágner, Martin
- Soudek, Petr
- Nepovím, Aleš
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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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is http://linked.open...avai/riv/vysledek
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