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FAD-containing polyamine oxidases: a timely challenge for researchers in biochemistry and physiology of plants

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F00%3A00001109" target="_blank" >RIV/61989592:15310/00:00001109 - isvavai.cz</a>

  • Alternative codes found

    RIV/61989592:15310/01:00001262

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    FAD-containing polyamine oxidases: a timely challenge for researchers in biochemistry and physiology of plants

  • Original language description

    Recent investigations on plant polyamine oxidase (PAO) are reviewed. The enzyme belongs to a new class of flavoenzymes with similar structural features including, among others, monoamine oxidase. Plant PAOs catalyse the oxidation of the polyamine substrates spermidine and spermine. The reaction products are propane-1,3-diamine and 1-pyrroline or 1-(3-aminopropyl)pyrroline, respectively, along with hydrogen peroxide. Plant PAOs are predominantly localised in the cell wall. Purification procedures and molecular properties of several plant PAOs are compared. A special attention is being paid to the recently solved crystal structure of the maize enzyme and its implications for the substrate binding and catalytic mechanism. Substrate specificity and inhibitors of plant PAOs are also described. The potential roles for PAO-generated H2O2 in lignin biosynthesis and cell wall cross-linking reactions, which may regulate growth and contribute to cell defence, are discussed.

  • Czech name

  • Czech description

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

    <a href="/en/project/GA203%2F97%2F0097" target="_blank" >GA203/97/0097: Molecular,structural and physiological properties of plant amine and cytokinine oxidases</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2001

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Plant Science

  • ISSN

    0168-9452

  • e-ISSN

  • Volume of the periodical

    160

  • Issue of the periodical within the volume

    NA

  • Country of publishing house

    XX - stateless person

  • Number of pages

    1

  • Pages from-to

  • UT code for WoS article

  • EID of the result in the Scopus database