Overproduction, Purification, and Characterization of Recombinant Aspartate Semialdehyde Dehydrogenase from Arabidopsis thaliana

In plant and microorganisms, aspartate semialdehyde dehydrogenase (ASDH) produces the branch point intermediate between the lysine and threonine/methionine pathways. In this study, we report the first cDNA cloning, purification, and characterization of a plant ASDH. The Arabidopsis thaliana ASDH is...

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Veröffentlicht in:	Protein expression and purification 2002-02, Vol.24 (1), p.99-104
Hauptverfasser:	Paris, Stephane, Wessel, Peter M., Dumas, Renaud
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis thaliana ASADH ASDH Aspartate-Semialdehyde Dehydrogenase - chemistry Aspartate-Semialdehyde Dehydrogenase - genetics Aspartate-Semialdehyde Dehydrogenase - isolation & purification Cloning, Molecular DNA, Complementary Escherichia coli - genetics Gene Expression Kinetics Molecular Sequence Data Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sequence Analysis, Protein Sequence Homology, Amino Acid Solutions
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Beschreibung
Zusammenfassung:	In plant and microorganisms, aspartate semialdehyde dehydrogenase (ASDH) produces the branch point intermediate between the lysine and threonine/methionine pathways. In this study, we report the first cDNA cloning, purification, and characterization of a plant ASDH. The Arabidopsis thaliana ASDH is an homodimeric enzyme composed of subunits of 36 kDa. The plant enzyme exhibited a specific activity of 26 μmol NADPH oxidized min−1 mg−1 of protein with a KM value for NADPH of 92 μM. ASDH showed cooperative behavior for aspartyl phosphate with a K0.5 value of 37 μM.
ISSN:	1046-5928 1096-0279
DOI:	10.1006/prep.2001.1538