About: 1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases     Goto   Sponge   Distinct   Permalink

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Description
  • Bylo zjištěno, že 1,5-diamino-2-pentin je substrátem i inaktivátorem rostlinné Cu aminooxidasy. (cs)
  • 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 intensity was s
  • 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 intensity was s (en)
Title
  • 1,5-diamino-2-pentin je substrátem i inaktivátorem rostlinné Cu aminooxidasy (cs)
  • 1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases
  • 1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases (en)
skos:prefLabel
  • 1,5-diamino-2-pentin je substrátem i inaktivátorem rostlinné Cu aminooxidasy (cs)
  • 1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases
  • 1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases (en)
skos:notation
  • RIV/61989592:15310/04:00002169!RIV/2005/MSM/153105/N
http://linked.open.../vavai/riv/strany
  • 4696-4708
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM 153100010)
http://linked.open...iv/cisloPeriodika
  • 23-24
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
  • 596529
http://linked.open...ai/riv/idVysledku
  • RIV/61989592:15310/04:00002169
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • amine oxidase;diamine;mechanism-based inhibition;nuclear magnetic resonance;oxidation (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • DE - Spolková republika Německo
http://linked.open...ontrolniKodProRIV
  • [E98821BE28E8]
http://linked.open...i/riv/nazevZdroje
  • European Journal of Biochemistry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 271
http://linked.open...iv/tvurceVysledku
  • Lemr, Karel
  • Šebela, Marek
  • Maloň, Michal
  • Lenobel, René
  • Peč, Pavel
  • Lamplot, Z.
  • Havlis, J.
  • Qiao, CH.
  • Sayre, L. M.
http://linked.open...n/vavai/riv/zamer
issn
  • 0014-2956
number of pages
http://localhost/t...ganizacniJednotka
  • 15310
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