Abstract
The first identification and characterization of a catalytic activity associated with NadR protein is reported. A computer-aided search for sequence similarity revealed the presence in NadR of a 29-residue region highly conserved among known nicotinamide mononucleotide adenylyltransferases. The Escherichia coli nadR gene was cloned into a T7-based vector and overexpressed. In addition to functionally specific DNA binding properties, the homogeneous recombinant protein catalyzes NAD synthesis from nicotinamide mononucleotide and ATP.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins*
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Cloning, Molecular
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DNA / metabolism
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Escherichia coli
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Gene Expression
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Molecular Sequence Data
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Nicotinamide-Nucleotide Adenylyltransferase / metabolism*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Repressor Proteins / genetics
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Repressor Proteins / isolation & purification
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Repressor Proteins / metabolism*
Substances
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Bacterial Proteins
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NadR protein, bacteria
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Recombinant Fusion Proteins
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Repressor Proteins
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DNA
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Nicotinamide-Nucleotide Adenylyltransferase