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Purification, crystallization and preliminary crystallographic study of a recombinant plant aminoaldehyde dehydrogenase from Pisum sativum
M Tylichova, P Briozzo, D Kopecny, J Ferrero, S Morera, N Joly, J Snegaroff, M Sebela
Language English Country Great Britain
NLK
Free Medical Journals
from 2005 to 2013
PubMed Central
from 2005 to 2013
Europe PubMed Central
from 2005 to 2013
Wiley Online Library (archiv)
from 2005-01-01 to 2012-12-31
- MeSH
- Aldehyde Dehydrogenase chemistry isolation & purification metabolism MeSH
- DNA Primers MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Financing, Organized MeSH
- Pisum sativum enzymology MeSH
- Cloning, Molecular MeSH
- Protein Conformation MeSH
- Crystallization MeSH
- Crystallography, X-Ray MeSH
- Recombinant Proteins chemistry isolation & purification metabolism MeSH
- Base Sequence MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Blotting, Western MeSH
Aminoaldehydes are products of polyamine degradation and are known to be reactive metabolites that are toxic to living cells at high concentrations. These compounds are catabolized by aminoaldehyde dehydrogenases, which are enzymes that contain a nicotinamide adenine dinucleotide coenzyme. Aminoaldehyde dehydrogenase from Pisum sativum was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop method. A complete data set was collected to 2.8 A resolution at 100 K. Crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 86.4, b = 216.6, c = 205.4 A, beta = 98.1 degrees. Molecular replacement was performed and led to the identification of six dimers per asymmetric unit.
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- $a eng
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- $a Tylichová, Martina. $7 _AN049555
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- $a Purification, crystallization and preliminary crystallographic study of a recombinant plant aminoaldehyde dehydrogenase from Pisum sativum / $c M Tylichova, P Briozzo, D Kopecny, J Ferrero, S Morera, N Joly, J Snegaroff, M Sebela
- 314 __
- $a Department of Biochemistry, Faculty of Science, Palacky University, Slechtitelu 11, CZ-78371 Olomouc, Czech Republic.
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- $a Aminoaldehydes are products of polyamine degradation and are known to be reactive metabolites that are toxic to living cells at high concentrations. These compounds are catabolized by aminoaldehyde dehydrogenases, which are enzymes that contain a nicotinamide adenine dinucleotide coenzyme. Aminoaldehyde dehydrogenase from Pisum sativum was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop method. A complete data set was collected to 2.8 A resolution at 100 K. Crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 86.4, b = 216.6, c = 205.4 A, beta = 98.1 degrees. Molecular replacement was performed and led to the identification of six dimers per asymmetric unit.
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- $a aldehyddehydrogenasa $x chemie $x izolace a purifikace $x metabolismus $7 D000444
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- $a elektroforéza v polyakrylamidovém gelu $7 D004591
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- $a hrách setý $x enzymologie $7 D018532
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- $a Briozzo, Pierre
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- $a Ferrero, Julien
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- $t Acta Crystallographica. Section F, Structural Biology & Crystallization Communications $w MED00179506 $g Roč. 64, č. Pt 2 (2008), s. 88-90
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- $a 2011-3B/vtme
