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

FEBS Letters

Ruggieri, Silverio²  Emanuelli, Monica¹  Lorenzi, Teresa¹  Amici, Adolfo¹  Raffaelli, Nadia¹  Magni, Giulio¹ 

[1] Istituto di Biochimica, Facoltà di Medicina e Chirurgia, University of Ancona, via Ranieri, 60100 Ancona, Italy;Dipartimento di Biotecnologie Agrarie ed Ambientali, University of Ancona, via Ranieri, 60100 Ancona, Italy

关键词: Adenylyltransferase;    Nudix hydrolase;    NAD biosynthesis;    Cyanobacterium;    Expression;   

DOI  :  10.1016/S0014-5793(99)00068-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown