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Molecular characterization and kinetic properties of a novel two-domain taurocyamine kinase from the lung fluke Paragonimus westermani |
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| Authors: | Blanca R Jarilla Mitsuru Nagataki Kouji Uda Takeshi Agatsuma |
| Institution: | a Department of Environmental Health Sciences, Kochi Medical School, Oko, Nankoku City, Kochi 783-8505, Japan b Department of Medical Environmental Biology, Chung-Ang University College of Medicine, Seoul, Republic of Korea c Laboratory of Biochemistry, Faculty of Science, Kochi University, Kochi 780-8520, Japan |
| Abstract: | Taurocyamine kinase (TK) was previously reported to be restricted to certain marine annelids; however, the present study has proven otherwise. The lung fluke Paragonimuswestermani has a contiguous two-domain TK with a mass of 80 216 Da consisting of 713 amino acid residues sharing higher sequence identity with molluscan arginine kinase (AK). Both domains of P. westermani TK have significant activity for the substrate taurocyamine and exhibited synergism during substrate binding. Since TK plays a key role in energy metabolism and is not present in mammals, inhibitors against P. westermani TK could be effective novel chemotherapeutic agents and could be utilized for the development of specific diagnostic tools for the detection of paragonimiasis. |
| Keywords: | PK phosphagen kinase TK taurocyamine kinase AK arginine kinase CK creatine kinase GK glycocyamine kinase LK lombricine kinase |
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