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Recent news related to substrates and inhibitors of plant copper amine oxidases

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F02%3A00001661" target="_blank" >RIV/61989592:15310/02:00001661 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Recent news related to substrates and inhibitors of plant copper amine oxidases

  • Original language description

    Plant copper amine oxidases (CAOs; EC 1.4.3.6) belong to the quinoprotein family. Besides the cofactor topaquinone, they also contain cupric ions participating in the reaction. Numerous substrates and inhibitors of plant CAOs have been reported up to date. We studied interactions of pea seedling enzyme (PSAO) with several artificial amine compounds that have not yet been analysed in this way and whose structure mimic natural polyamine substrates. In addition, our attention was paid to the evaluation ofinhibition potency of sedamine alkaloids and various pyridine-derived oximes. 1,4-Bis(3-aminopropyl)piperazine, N,N´-bis(3-aminopropyl)-trans-2-butene-1,4-diamine and 3-oxapentane-1,5-diamine (OPD) were found to be substrates of PSAO. The corresponding enzyme kinetics was measured, the reaction stoichiometry analysed and rapid-scanning spectrophotometry applied to investigate the reaction mechanism. The identity of the main product of OPD conversion was confirmed by several analytical me

  • Czech name

  • Czech description

Classification

  • Type

    D - Article in proceedings

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GA203%2F00%2FD119" target="_blank" >GA203/00/D119: Structure and properties of endogenous amine oxidase inhibitor from bean seedlings and its analogues</a><br>

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2002

  • Confidentiality

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

Data specific for result type

  • Article name in the collection

    30rd International Symposium on Vitamin B6, PQQ, Carbonyl Catalysis and quinoproteins

  • ISBN

  • ISSN

  • e-ISSN

  • Number of pages

    60

  • Pages from-to

    37

  • Publisher name

    University of Southampton

  • Place of publication

    Southampton

  • Event location

    Southampton

  • Event date

  • Type of event by nationality

    EUR - Evropská akce

  • UT code for WoS article