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1,5-diamino-2-pentyne is both a substrate and inactivator 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%2F04%3A00002169" target="_blank" >RIV/61989592:15310/04:00002169 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases

  • Original language description

    1,5-Diamino-2-pentyne (DAPY) was found to be a weak substrate of grass pea (Lathyrus sativus, GPAO) and sainfoin (Onobrychis viciifolia, OVAO) amine oxidases. Prolonged incubations, however, resulted in irreversible inhibition of both enzymes. For GPAO and OVAO, rates of inactivation of 0.1-0.3 min(-1) were determined, the apparent K-I values (half-maximal inactivation) were of the order of 10(-5) M. DAPY was found to be a mechanism-based inhibitor of the enzymes because the substrate cadaverine significantly prevented irreversible inhibition. The N-1-methyl and N-5-methyl analogs of DAPY were tested with GPAO and were weaker inactivators (especially the N-5-methyl) than DAPY. Prolonged incubations of GPAO or OVAO with DAPY resulted in the appearance of a yellow-brown chromophore (lambda(max) = 310-325 nm depending on the working buffer). Excitation at 310 nm was associated with emitted fluorescence with a maximum at 445 nm, suggestive of extended conjugation. After dialysis, the color

  • Czech name

    1,5-diamino-2-pentin je substrátem i inaktivátorem rostlinné Cu aminooxidasy

  • Czech description

    Bylo zjištěno, že 1,5-diamino-2-pentin je substrátem i inaktivátorem rostlinné Cu aminooxidasy.

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2004

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    European Journal of Biochemistry

  • ISSN

    0014-2956

  • e-ISSN

  • Volume of the periodical

    271

  • Issue of the periodical within the volume

    23-24

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    13

  • Pages from-to

    4696-4708

  • UT code for WoS article

  • EID of the result in the Scopus database