Development in the course of study substrates and inhibitors of plant copper amine oxidases

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F02%3A00001609" target="_blank" >RIV/61989592:15310/02:00001609 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Development in the course of study substrates and inhibitors of plant copper amine oxidases
Original language description
Plant copper amine oxidases (CuAOS; EC 1. 4. 3. 6) belong to the quinoprotein family. Besides the cofactor topaquinone, they also contain cupric ions participating in the reaction. They catalyse the oxidative deamination of amine substrates to the respective aldehydes, ammonia and hydrogen peroxide (MEDDA, 1995). We studied interactions of pea seedling enzyme (PSAO) with several artifical amine compounds that have not yet been analysed in this way and whose structure mimic natural polyamine substrates.In the second part we focused our attention on the interaction of optically active sedamine alkaloids and various pyridine-derived oximes with PSAO. 3-Oxapentane-1,5-diamine (OPD), 1, 4-bis-(3-aminopropyl)piperazine and N, N-bis(3-aminopropyl)-trans-2-butene were found to be substrates of PSAO. The corresponding enzyme kinetics was measured, the reaction stechiometry analysed and rapid scanning spectrophotometry applied to investigate the reaction mechanism. A similar compound to OPD, 3-
Czech name
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Czech description
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Publication year
2002
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Article name in the collection
18th Joint Congress of the Czech and Slovak Societies for Biochemistry and Molecular Biology
ISBN
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ISSN
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e-ISSN
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Number of pages
410
Pages from-to
110
Publisher name
Slovenská spoločnosť pre biochémiu a molekulárnu biológiu
Place of publication
Bratislava
Event location
Stará Lesná
Event date
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Type of event by nationality
EUR - Evropská akce
UT code for WoS article
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