About: Development in the course of study substrates and inhibitors of plant copper amine oxidases     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
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-azapentane-1,5-d
  • 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-azapentane-1,5-d (en)
Title
  • Development in the course of study substrates and inhibitors of plant copper amine oxidases
  • Development in the course of study substrates and inhibitors of plant copper amine oxidases (en)
skos:prefLabel
  • Development in the course of study substrates and inhibitors of plant copper amine oxidases
  • Development in the course of study substrates and inhibitors of plant copper amine oxidases (en)
skos:notation
  • RIV/61989592:15310/02:00001609!RIV/2003/MSM/153103/N
http://linked.open.../vavai/riv/strany
  • 110
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM 153100010)
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 642843
http://linked.open...ai/riv/idVysledku
  • RIV/61989592:15310/02:00001609
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • amine; amine oxidase; enzyme; inhibitor; substrate (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [DE45D5EBA304]
http://linked.open...v/mistoKonaniAkce
  • Stará Lesná
http://linked.open...i/riv/mistoVydani
  • Bratislava
http://linked.open...i/riv/nazevZdroje
  • 18th Joint Congress of the Czech and Slovak Societies for Biochemistry and Molecular Biology
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...ocetUcastnikuAkce
http://linked.open...nichUcastnikuAkce
http://linked.open...UplatneniVysledku
http://linked.open...iv/tvurceVysledku
  • Lemr, Karel
  • Petřivalský, Marek
  • Šebela, Marek
  • Frébort, Ivo
  • Adámková, Šárka
  • Peč, Pavel
  • Mlíčková, Kateřina
  • Lamplot, Zbyněk
http://linked.open...vavai/riv/typAkce
http://linked.open...n/vavai/riv/zamer
number of pages
http://purl.org/ne...btex#hasPublisher
  • Slovenská spoločnosť pre biochémiu a molekulárnu biológiu pri SAV
http://localhost/t...ganizacniJednotka
  • 15310
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 38 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software