TAILIEUCHUNG - Báo cáo khoa học: A novel nucleoside kinase from Burkholderia thailandensis A member of the phosphofructokinase B-type family of enzymes

The genome of the mesophilic Gram-negative bacteriumBurkholderia thai-landensis contains an open reading frame (. theBth_I1158gene) that has been annotated as a putative ribokinase and PFK-B family member. Nota-bly, although the deduced amino acid sequence of the gene showed only 29% similarity to the recently identified nucleoside kinase from hyperthermophilic archaeaMethanocaldococcus jannaschii, 15 of 17 residues reportedly involved in the catalytic activity of M. | ỊFEBS Journal A novel nucleoside kinase from Burkholderia thailandensis A member of the phosphofructokinase B-type family of enzymes Hiroko Ota1 Shin-ichi Sakasegawa1 Yuko Yasuda1 Shigeyuki Imamura1 and Tomohiro Tamura2 3 1 Asahi Kasei Pharma Corporation Shizuoka Japan 2 Research Institute of Genome-based Biofactory NationalInstitute of Advanced IndustrialSciences and Technology AIST Sapporo Japan 3 Laboratory of Molecular EnvironmentalMicrobiology Graduate Schoolof Agriculture Hokkaido University Japan Keywords adenosine kinase Burkholderia thailandensis inosine guanosine kinase nucleoside kinase phosphofructokinase B Correspondence S. Sakasegawa Asahi Kasei Pharma Corporation Shizuoka 410-4321 Japan Fax 81 0558 76 7149 Tel 81 0558 76 8564 E-mail Received 13 August 2008 revised 24 September 2008 accepted 29 September 2008 doi The genome of the mesophilic Gram-negative bacterium Burkholderia thai-landensis contains an open reading frame . the Bth_I1158 gene that has been annotated as a putative ribokinase and PFK-B family member. Notably although the deduced amino acid sequence of the gene showed only 29 similarity to the recently identified nucleoside kinase from hyperthermophilic archaea Methanocaldococcus jannaschii 15 of 17 residues reportedly involved in the catalytic activity of M. jannaschii nucleoside kinase were conserved. The gene was cloned and functionally overexpressed in Rhodococcus erythropolis and the purified enzyme was characterized biochemically. The substrate specificity of the enzyme was unusually broad for a bacterial PFK-B protein and the specificity extended not only to purine and purine-analog nucleosides but also to uridine. Inosine was the most effective phosphoryl acceptor with the highest kcat Km value 80 s-1-mM-1 being achieved when ATP served as the phosphoryl donor. By contrast this enzyme exhibited no activity toward ribose indicating that the recombinant enzyme

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