Synechocystis sp. slr0787 protein is a novel bifunctional enzyme endowed with both nicotinamide mononucleotide adenylyltransferase and ‘Nudix' hydrolase activities

Abstract
Synechocystis sp. slr0787 open reading frame encodes a 339 residue polypeptide with a predicted molecular mass of 38.5 kDa. Its deduced amino acid sequence shows extensive homology with known separate sequences of proteins from the thermophilic archaeon Methanococcus jannaschii. The N‐terminal domain is highly homologous to the archaeal NMN adenylyltransferase, which catalyzes NAD synthesis from NMN and ATP. The C‐terminal domain shares homology with the archaeal ADP‐ribose pyrophosphatase, a member of the ‘Nudix' hydrolase family. The slr0787 gene has been cloned into a T7‐based vector for expression in Escherichia coli cells. The recombinant protein has been purified to homogeneity and demonstrated to possess both NMN adenylyltransferase and ADP‐ribose pyrophosphatase activities. Both activities have been characterized and compared to their archaeal counterparts.

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