The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst
Abstract
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 Rhipicephalus sanguineus (Rs), the vector for Rocky Mountain Spotted Fever. 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. The Michaelis-Menten kinetics confirmed that RsAK is an efficient biocatalyst due to its high kcat/Km 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 RsAK enzymatic inhibition that may lead to novel strategies to control this pest, a burden to animal and human health.
- Publication Date:
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1891582
- Grant/Contract Number:
- AC02-76SF00515
- Resource Type:
- Published Article
- Journal Name:
- Catalysts
- Additional Journal Information:
- Journal Name: Catalysts Journal Volume: 12 Journal Issue: 10; Journal ID: ISSN 2073-4344
- Publisher:
- MDPI AG
- Country of Publication:
- Switzerland
- Language:
- English
Citation Formats
Gomez-Yanes, Ana C., Moreno-Cordova, Elena N., Garcia-Orozco, Karina D., Laino, Aldana, Islas-Osuna, Maria A., Lopez-Zavala, Alonso A., Valenzuela, Jesus G., and Sotelo-Mundo, Rogerio R. The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst. Switzerland: N. p., 2022.
Web. doi:10.3390/catal12101178.
Gomez-Yanes, Ana C., Moreno-Cordova, Elena N., Garcia-Orozco, Karina D., Laino, Aldana, Islas-Osuna, Maria A., Lopez-Zavala, Alonso A., Valenzuela, Jesus G., & Sotelo-Mundo, Rogerio R. The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst. Switzerland. https://doi.org/10.3390/catal12101178
Gomez-Yanes, Ana C., Moreno-Cordova, Elena N., Garcia-Orozco, Karina D., Laino, Aldana, Islas-Osuna, Maria A., Lopez-Zavala, Alonso A., Valenzuela, Jesus G., and Sotelo-Mundo, Rogerio R. Thu .
"The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst". Switzerland. https://doi.org/10.3390/catal12101178.
@article{osti_1891582,
title = {The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst},
author = {Gomez-Yanes, Ana C. and Moreno-Cordova, Elena N. and Garcia-Orozco, Karina D. and Laino, Aldana and Islas-Osuna, Maria A. and Lopez-Zavala, Alonso A. and Valenzuela, Jesus G. and Sotelo-Mundo, Rogerio R.},
abstractNote = {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 Rhipicephalus sanguineus (Rs), the vector for Rocky Mountain Spotted Fever. 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. The Michaelis-Menten kinetics confirmed that RsAK is an efficient biocatalyst due to its high kcat/Km 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 RsAK enzymatic inhibition that may lead to novel strategies to control this pest, a burden to animal and human health.},
doi = {10.3390/catal12101178},
journal = {Catalysts},
number = 10,
volume = 12,
place = {Switzerland},
year = {Thu Oct 06 00:00:00 EDT 2022},
month = {Thu Oct 06 00:00:00 EDT 2022}
}
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