Abstract:
:The enzyme nicotinamide mononucleotide (NMN) adenylyltransferase (EC 2.7.7.1) catalyzes the synthesis of NAD+ and nicotinic acid adenine dinucleotide. It has been purified to homogeneity from cellular extracts of the thermophilic archaeon Sulfolobus solfataricus. Through a database search, a highly significant match was found between its N-terminal sequence and a hypothetical protein coded by the thermophilic archaeon Methanococcus jannaschii MJ0541 open reading frame (GenBank accession no. U67503). The MJ0541 gene was isolated, cloned into a T7-based vector, and expressed in Escherichia coli cells, yielding a high level of thermophilic NMN adenylyltransferase activity. The expressed protein was purified to homogeneity by a single-step chromatographic procedure. Both the subunit molecular mass and the N-terminal sequence of the pure recombinant protein were as expected from the deduced amino acid sequence of the MJ0541 open reading frame-encoded protein. Molecular and kinetic properties of the enzymes from both archaea are reported and compared with those already known for the mesophilic eukaryotic NMN adenylyltransferase.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Raffaelli N,Pisani FM,Lorenzi T,Emanuelli M,Amici A,Ruggieri S,Magni Gdoi
10.1128/jb.179.24.7718-7723.1997subject
Has Abstractpub_date
1997-12-01 00:00:00pages
7718-23issue
24eissn
0021-9193issn
1098-5530journal_volume
179pub_type
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