![]() To date, there are algorithms capable of predicting both linear and discontinuous epitopes. Future work will be focused on the RsAK enzymatic inhibition that may lead to novel strategies to control this pest, a burden to animal and human health.Īntigenic sites are essential since these enzymes are proteins that may elicit an immune response, such as allergens. AK is an essential enzyme in invertebrates. The recombinant enzyme was expressed in bacteria and purified to a 20 mg/L culture yield. ![]() The Michaelis-Menten kinetics confirmed that RsAK is an efficient biocatalyst due to its high k cat/ K m parameter. Here we report the enzymatic activity and the crystal structure of AK from Rhipicephalus sanguineus ( RsAK) in an open conformation without substrate or ligands and a theoretical structure of RsAK modeled bound with the substrate/product (Arg-ADP) in a closed conformation. Although AK has been primarily described in the shrimp, it is also present in other invertebrates, such as the brown tick Rhipicephalus sanguineus ( Rs), the vector for Rocky Mountain Spotted Fever. AK also elicits an immune response in humans, and it is a major food allergen in crustacea and may be a target for novel antiparasitic drugs. ![]() Arginine kinase (AK) is a reversible enzyme that regulates invertebrates’ phosphagen arginine phosphate levels.
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