The Escherichia coli NadR Regulator Is Endowed with Nicotinamide Mononucleotide Adenylyltransferase Activity
AUTOR(ES)
Raffaelli, Nadia
FONTE
American Society for Microbiology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=94063Documentos Relacionados
- NAD-Dependent DNA-Binding Activity of the Bifunctional NadR Regulator of Salmonella typhimurium
- Regulation of NAD metabolism in Salmonella typhimurium: molecular sequence analysis of the bifunctional nadR regulator and the nadA-pnuC operon.
- Identification of the nicotinamide mononucleotide adenylyltransferase of Trypanosoma cruzi
- Characterization of nicotinamide mononucleotide adenylyltransferase from thermophilic archaea.
- Identification of the Escherichia coli Nicotinic Acid Mononucleotide Adenylyltransferase Gene