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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F04%3A00002169%21RIV%2F2005%2FMSM%2F153105%2FN
rdf:type
skos:Concept n15:Vysledek
dcterms: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 intensity was s Bylo zjištěno, že 1,5-diamino-2-pentin je substrátem i inaktivátorem rostlinné Cu aminooxidasy. 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
dcterms:title
1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases 1,5-diamino-2-pentin je substrátem i inaktivátorem rostlinné Cu aminooxidasy 1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases
skos:prefLabel
1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases 1,5-diamino-2-pentin je substrátem i inaktivátorem rostlinné Cu aminooxidasy 1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases
skos:notation
RIV/61989592:15310/04:00002169!RIV/2005/MSM/153105/N
n3:strany
4696-4708
n3:aktivita
n9:Z
n3:aktivity
Z(MSM 153100010)
n3:cisloPeriodika
23-24
n3:dodaniDat
n13:2005
n3:domaciTvurceVysledku
n12:9896821 n12:4316851 n12:5433851 n12:9708790 n12:4396626
n3:druhVysledku
n14:J
n3:duvernostUdaju
n11:S
n3:entitaPredkladatele
n5:predkladatel
n3:idSjednocenehoVysledku
596529
n3:idVysledku
RIV/61989592:15310/04:00002169
n3:jazykVysledku
n18:eng
n3:klicovaSlova
amine oxidase;diamine;mechanism-based inhibition;nuclear magnetic resonance;oxidation
n3:klicoveSlovo
n10:mechanism-based%20inhibition n10:oxidation n10:nuclear%20magnetic%20resonance n10:amine%20oxidase n10:diamine
n3:kodStatuVydavatele
DE - Spolková republika Německo
n3:kontrolniKodProRIV
[E98821BE28E8]
n3:nazevZdroje
European Journal of Biochemistry
n3:obor
n4:CE
n3:pocetDomacichTvurcuVysledku
5
n3:pocetTvurcuVysledku
9
n3:rokUplatneniVysledku
n13:2004
n3:svazekPeriodika
271
n3:tvurceVysledku
Havlis, J. Peč, Pavel Lenobel, René Šebela, Marek Maloň, Michal Sayre, L. M. Lamplot, Z. Lemr, Karel Qiao, CH.
n3:zamer
n17:MSM%20153100010
s:issn
0014-2956
s:numberOfPages
13
n16:organizacniJednotka
15310