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Statements

Subject Item
n2:RIV%2F61389030%3A_____%2F10%3A00359314%21RIV11-GA0-61389030
rdf:type
n4:Vysledek skos:Concept
dcterms: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.
dcterms: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
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
skos:notation
RIV/61389030:_____/10:00359314!RIV11-GA0-61389030
n6:aktivita
n7:Z n7:P
n6:aktivity
P(GA301/08/1649), P(GA522/08/0555), Z(AV0Z50380511), Z(MSM6198959215)
n6:cisloPeriodika
4
n6:dodaniDat
n9:2011
n6:domaciTvurceVysledku
n15:9896821
n6:druhVysledku
n13:J
n6:duvernostUdaju
n10:S
n6:entitaPredkladatele
n18:predkladatel
n6:idSjednocenehoVysledku
290413
n6:idVysledku
RIV/61389030:_____/10:00359314
n6:jazykVysledku
n17:eng
n6:klicovaSlova
aminoaldehyde dehydrogenase; betaine aldehyde dehydrogenase; NAD+ complex
n6:klicoveSlovo
n16:NAD%2B%20complex n16:betaine%20aldehyde%20dehydrogenase n16:aminoaldehyde%20dehydrogenase
n6:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n6:kontrolniKodProRIV
[B3DBC0872824]
n6:nazevZdroje
Journal of Molecular Biology
n6:obor
n8:CE
n6:pocetDomacichTvurcuVysledku
1
n6:pocetTvurcuVysledku
7
n6:projekt
n14:GA522%2F08%2F0555 n14:GA301%2F08%2F1649
n6:rokUplatneniVysledku
n9:2010
n6:svazekPeriodika
396
n6:tvurceVysledku
Kopečný, D. Tylichová, M. Briozzo, P. Šebela, M. Snégaroff, J. Lenobel, René Moréra, S.
n6:wos
000275385600005
n6:zamer
n12:MSM6198959215 n12:AV0Z50380511
s:issn
0022-2836
s:numberOfPages
13