The Escherichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity.
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.
Raffaelli
N
N
Istituto di Biochimica, Facoltà di Medicina, Università di Ancona, 60131 Ancona, Italy.
Lorenzi
T
T
Mariani
P L
PL
Emanuelli
M
M
Amici
A
A
Ruggieri
S
S
Magni
G
G
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism; D004926:Escherichia coli; D015870:Gene Expression; D008969:Molecular Sequence Data; D009612:Nicotinamide-Nucleotide Adenylyltransferase / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D012097:Repressor Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D001426:Bacterial Proteins; C117105:NadR protein, bacteria; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; D004247:DNA; D009612:Nicotinamide-Nucleotide Adenylyltransferase