AI Article Synopsis
- The study reveals that taurocyamine kinase (TK), previously believed to be specific to certain marine annelids, is also found in the lung fluke Paragonimus westermani.
- P. westermani's TK has a unique structure with two domains, sharing similarities to molluscan arginine kinase and showing strong activity for taurocyamine, enhancing substrate binding.
- Targeting P. westermani TK with inhibitors could lead to new treatments for infections and aid in the development of diagnostic methods for paragonimiasis.
Article Abstract
Taurocyamine kinase (TK) was previously reported to be restricted to certain marine annelids; however, the present study has proven otherwise. The lung fluke Paragonimus westermani has a contiguous two-domain TK with a mass of 80216 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.
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| http://dx.doi.org/10.1016/j.febslet.2009.05.049 | DOI Listing |
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