Abstract
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 micromol NADPH oxidized min(-1) mg(-1) of protein with a K(M) value for NADPH of 92 microM. ASDH showed cooperative behavior for aspartyl phosphate with a K(0.5) value of 37 microM.
Copyright 2002 Elsevier Science (USA).
MeSH terms
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Amino Acid Sequence
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Arabidopsis / enzymology*
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Arabidopsis / genetics
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Aspartate-Semialdehyde Dehydrogenase / chemistry
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Aspartate-Semialdehyde Dehydrogenase / genetics*
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Aspartate-Semialdehyde Dehydrogenase / isolation & purification
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Cloning, Molecular*
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DNA, Complementary
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Escherichia coli / genetics
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Gene Expression
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Kinetics
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Molecular Sequence Data
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Sequence Analysis, Protein
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Sequence Homology, Amino Acid
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Solutions
Substances
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DNA, Complementary
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Recombinant Proteins
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Solutions
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Aspartate-Semialdehyde Dehydrogenase