The Arginine Kinase from the Tick <i>Rhipicephalus sanguineus</i> Is an Efficient Biocatalyst
Arginine kinase (AK) is a reversible enzyme that regulates invertebrates’ phosphagen arginine phosphate levels. 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. Although AK has been primarily described in th...
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MDPI AG
2022-10-01
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| author | Ana C. Gomez-Yanes Elena N. Moreno-Cordova Karina D. Garcia-Orozco Aldana Laino Maria A. Islas-Osuna Alonso A. Lopez-Zavala Jesus G. Valenzuela Rogerio R. Sotelo-Mundo |
| author_facet | Ana C. Gomez-Yanes Elena N. Moreno-Cordova Karina D. Garcia-Orozco Aldana Laino Maria A. Islas-Osuna Alonso A. Lopez-Zavala Jesus G. Valenzuela Rogerio R. Sotelo-Mundo |
| author_sort | Ana C. Gomez-Yanes |
| collection | DOAJ |
| description | Arginine kinase (AK) is a reversible enzyme that regulates invertebrates’ phosphagen arginine phosphate levels. 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. Although AK has been primarily described in the shrimp, it is also present in other invertebrates, such as the brown tick <i>Rhipicephalus sanguineus</i> (<i>Rs</i>), the vector for Rocky Mountain Spotted Fever. Here we report the enzymatic activity and the crystal structure of AK from <i>Rhipicephalus sanguineus</i> (<i>Rs</i>AK) in an open conformation without substrate or ligands and a theoretical structure of <i>Rs</i>AK modeled bound with the substrate/product (Arg-ADP) in a closed conformation. The Michaelis-Menten kinetics confirmed that <i>Rs</i>AK is an efficient biocatalyst due to its high <i>k<sub>cat</sub></i>/<i>K<sub>m</sub></i> parameter. The recombinant enzyme was expressed in bacteria and purified to a 20 mg/L culture yield. AK is an essential enzyme in invertebrates. Future work will be focused on the <i>Rs</i>AK enzymatic inhibition that may lead to novel strategies to control this pest, a burden to animal and human health. |
| first_indexed | 2024-03-09T20:30:04Z |
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| id | doaj.art-620e93869af44a599a47b89a5466ab46 |
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| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-09T20:30:04Z |
| publishDate | 2022-10-01 |
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| series | Catalysts |
| spelling | doaj.art-620e93869af44a599a47b89a5466ab462023-11-23T23:24:57ZengMDPI AGCatalysts2073-43442022-10-011210117810.3390/catal12101178The Arginine Kinase from the Tick <i>Rhipicephalus sanguineus</i> Is an Efficient BiocatalystAna C. Gomez-Yanes0Elena N. Moreno-Cordova1Karina D. Garcia-Orozco2Aldana Laino3Maria A. Islas-Osuna4Alonso A. Lopez-Zavala5Jesus G. Valenzuela6Rogerio R. Sotelo-Mundo7Laboratorio de Estructura Biomolecular, Centro de Investigación en Alimentación y Desarrollo, A.C., Carretera Gustavo Enrique Astiazarán Rosas Núm. 46, Ejido a La Victoria, Hermosillo 83304, Sonora, MexicoLaboratorio de Estructura Biomolecular, Centro de Investigación en Alimentación y Desarrollo, A.C., Carretera Gustavo Enrique Astiazarán Rosas Núm. 46, Ejido a La Victoria, Hermosillo 83304, Sonora, MexicoLaboratorio de Estructura Biomolecular, Centro de Investigación en Alimentación y Desarrollo, A.C., Carretera Gustavo Enrique Astiazarán Rosas Núm. 46, Ejido a La Victoria, Hermosillo 83304, Sonora, MexicoInstituto de Investigaciones Bioquímicas de La Plata “Dr. Prof. Rodolfo R. Brenner” (INIBIOLP), Centro Cientifico Tecnologico-La Plata CONICET-Universidad Nacional de La Plata, Calle 60 y 120, La Plata 1900, ArgentinaLaboratorio de Genética y Biología Molecular de Plantas, Centro de Investigación en Alimentación y Desarrollo, A.C., Carretera Gustavo Enrique Astiazarán Rosas Núm. 46, Ejido a La Victoria, Hermosillo 83304, Sonora, MexicoDepartamento de Ciencias Quimico Biológicas, Universidad de Sonora, Blvd. Rosales y Bvd. Luis Encinas s/n., Hermosillo 83000, Sonora, MexicoVector Molecular Biology Section, Laboratory of Malaria and Vector Research, 5601 Fishers Ln, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852, USALaboratorio de Estructura Biomolecular, Centro de Investigación en Alimentación y Desarrollo, A.C., Carretera Gustavo Enrique Astiazarán Rosas Núm. 46, Ejido a La Victoria, Hermosillo 83304, Sonora, MexicoArginine kinase (AK) is a reversible enzyme that regulates invertebrates’ phosphagen arginine phosphate levels. 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. Although AK has been primarily described in the shrimp, it is also present in other invertebrates, such as the brown tick <i>Rhipicephalus sanguineus</i> (<i>Rs</i>), the vector for Rocky Mountain Spotted Fever. Here we report the enzymatic activity and the crystal structure of AK from <i>Rhipicephalus sanguineus</i> (<i>Rs</i>AK) in an open conformation without substrate or ligands and a theoretical structure of <i>Rs</i>AK modeled bound with the substrate/product (Arg-ADP) in a closed conformation. The Michaelis-Menten kinetics confirmed that <i>Rs</i>AK is an efficient biocatalyst due to its high <i>k<sub>cat</sub></i>/<i>K<sub>m</sub></i> parameter. The recombinant enzyme was expressed in bacteria and purified to a 20 mg/L culture yield. AK is an essential enzyme in invertebrates. Future work will be focused on the <i>Rs</i>AK enzymatic inhibition that may lead to novel strategies to control this pest, a burden to animal and human health.https://www.mdpi.com/2073-4344/12/10/1178arginine kinaseenzymeallergentickcrystal structureepitopes |
| spellingShingle | Ana C. Gomez-Yanes Elena N. Moreno-Cordova Karina D. Garcia-Orozco Aldana Laino Maria A. Islas-Osuna Alonso A. Lopez-Zavala Jesus G. Valenzuela Rogerio R. Sotelo-Mundo The Arginine Kinase from the Tick <i>Rhipicephalus sanguineus</i> Is an Efficient Biocatalyst Catalysts arginine kinase enzyme allergen tick crystal structure epitopes |
| title | The Arginine Kinase from the Tick <i>Rhipicephalus sanguineus</i> Is an Efficient Biocatalyst |
| title_full | The Arginine Kinase from the Tick <i>Rhipicephalus sanguineus</i> Is an Efficient Biocatalyst |
| title_fullStr | The Arginine Kinase from the Tick <i>Rhipicephalus sanguineus</i> Is an Efficient Biocatalyst |
| title_full_unstemmed | The Arginine Kinase from the Tick <i>Rhipicephalus sanguineus</i> Is an Efficient Biocatalyst |
| title_short | The Arginine Kinase from the Tick <i>Rhipicephalus sanguineus</i> Is an Efficient Biocatalyst |
| title_sort | arginine kinase from the tick i rhipicephalus sanguineus i is an efficient biocatalyst |
| topic | arginine kinase enzyme allergen tick crystal structure epitopes |
| url | https://www.mdpi.com/2073-4344/12/10/1178 |
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