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

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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	Z
http://linked.open...avai/riv/aktivity	Z(MSM 153100010)
http://linked.open...iv/cisloPeriodika	23-24
http://linked.open...vai/riv/dodaniDat	2005
http://linked.open...aciTvurceVysledku	Peč, Pavel Šebela, Marek Lemr, Karel Maloň, Michal Lenobel, René
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	596529
http://linked.open...ai/riv/idVysledku	RIV/61989592:15310/04:00002169
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	amine oxidase;diamine;mechanism-based inhibition;nuclear magnetic resonance;oxidation (en)
http://linked.open.../riv/klicoveSlovo	amine oxidase nuclear magnetic resonance oxidation mechanism-based inhibition diamine
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	CE
http://linked.open...ichTvurcuVysledku	5 (xsd:int)
http://linked.open...cetTvurcuVysledku	9 (xsd:int)
http://linked.open...UplatneniVysledku	2004
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	http://linked.opendata.cz/resource/domain/vavai/zamer/MSM%20153100010
issn	0014-2956
number of pages	13 (xsd:int)
http://localhost/t...ganizacniJednotka	15310

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