About: Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes

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About: Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Here, we report the first X-ray structures of plant AMADHs: two isoenzymes, PsAMADH1 and PsAMADH2, from Pisum sativum in complex with β-nicotinamide adenine dinucleotide (NAD+) at 2.4 and 2.15 Å resolution, respectively. Both recombinant proteins are dimeric. Each subunit binds NAD+ as a coenzyme, contains a solvent-accessible C-terminal peroxisomal targeting signal (type 1) and a cation bound in the cavity close to the NAD+ binding site. Structural analysis and substrate specificity study of both isoenzymes in combination with data published previously on other ALDH9 family members show that the established categorization of such enzymes into distinct groups based on substrate specificity is no more appropriate, because many of them seem capable of oxidizing a large spectrum of aminoaldehyde substrates. PsAMADH1 and PsAMADH2 can oxidize N,N,N-trimethyl-4-aminobutyraldehyde into γ-butyrobetaine, which is the carnitine precursor in animal cells. Here, we report the first X-ray structures of plant AMADHs: two isoenzymes, PsAMADH1 and PsAMADH2, from Pisum sativum in complex with β-nicotinamide adenine dinucleotide (NAD+) at 2.4 and 2.15 Å resolution, respectively. Both recombinant proteins are dimeric. Each subunit binds NAD+ as a coenzyme, contains a solvent-accessible C-terminal peroxisomal targeting signal (type 1) and a cation bound in the cavity close to the NAD+ binding site. Structural analysis and substrate specificity study of both isoenzymes in combination with data published previously on other ALDH9 family members show that the established categorization of such enzymes into distinct groups based on substrate specificity is no more appropriate, because many of them seem capable of oxidizing a large spectrum of aminoaldehyde substrates. PsAMADH1 and PsAMADH2 can oxidize N,N,N-trimethyl-4-aminobutyraldehyde into γ-butyrobetaine, which is the carnitine precursor in animal cells. (en)
Title	Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes (en)
skos:prefLabel	Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes (en)
skos:notation	RIV/61389030:_____/10:00359314!RIV11-GA0-61389030
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA301/08/1649), P(GA522/08/0555), Z(AV0Z50380511), Z(MSM6198959215)
http://linked.open...iv/cisloPeriodika	4
http://linked.open...vai/riv/dodaniDat	2011
http://linked.open...aciTvurceVysledku	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	Ústav experimentální botaniky AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	290413
http://linked.open...ai/riv/idVysledku	RIV/61389030:_____/10:00359314
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	aminoaldehyde dehydrogenase; betaine aldehyde dehydrogenase; NAD+ complex (en)
http://linked.open.../riv/klicoveSlovo	betaine aldehyde dehydrogenase aminoaldehyde dehydrogenase NAD+ complex
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[B3DBC0872824]
http://linked.open...i/riv/nazevZdroje	Journal of Molecular Biology
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	7 (xsd:int)
http://linked.open...vavai/riv/projekt	Modulation of cell division of normal and cancer cells by cyclin-dependent kinase inhibitors Structure-functional characterization of oxidoreductases acting on nitrogenous regulatory compounds in plants
http://linked.open...UplatneniVysledku	2010
http://linked.open...v/svazekPeriodika	396
http://linked.open...iv/tvurceVysledku	Šebela, M. Lenobel, René Briozzo, P. Kopečný, D. Moréra, S. Snégaroff, J. Tylichová, M.
http://linked.open...ain/vavai/riv/wos	000275385600005
http://linked.open...n/vavai/riv/zamer	Mechanismy regulace růstu a vývoje rostlin na úrovni buněk, orgánů a celých organismů: fyziologické, genetické a molekulárně biologické základy Variabilita složek a interakcí v rostlinném patosystému a vliv faktorů prostředí na jejich projev
issn	0022-2836
number of pages	13 (xsd:int)

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