The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst

Autores
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 Rafael
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Arginine kinase (AK) is a reversible enzyme that regulates invertebrates’ phosphagenarginine phosphate levels. AK also elicits an immune response in humans, and it is a major foodallergen in crustacea and may be a target for novel antiparasitic drugs. Although AK has beenprimarily described in the shrimp, it is also present in other invertebrates, such as the brown tickRhipicephalus sanguineus (Rs), the vector for Rocky Mountain Spotted Fever. Here we report theenzymatic activity and the crystal structure of AK from Rhipicephalus sanguineus (RsAK) in an openconformation without substrate or ligands and a theoretical structure of RsAK modeled bound withthe substrate/product (Arg-ADP) in a closed conformation. The Michaelis-Menten kinetics confirmedthat RsAK is an efficient biocatalyst due to its high kcat/Km parameter. The recombinant enzymewas expressed in bacteria and purified to a 20 mg/L culture yield. AK is an essential enzyme ininvertebrates. Future work will be focused on the RsAK enzymatic inhibition that may lead to novelstrategies to control this pest, a burden to animal and human health.
Fil: Gomez Yanes, Ana C.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Moreno Cordova, Elena N.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Garcia Orozco, Karina D.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Laino, Aldana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Islas Osuna, Maria A.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Lopez Zavala, Alonso A.. Universidad de Sonora; México
Fil: Valenzuela, Jesus G.. Universidad de Sonora; México
Fil: Sotelo Mundo, Rogerio Rafael. Centro de Investigación E/alimentos y Desarrollo A.c; México
Materia
ARGININE KINASE
ENZIME
ALLLERGEN
TICK
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/240944
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/240944
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient BiocatalystGomez Yanes, Ana C.Moreno Cordova, Elena N.Garcia Orozco, Karina D.Laino, AldanaIslas Osuna, Maria A.Lopez Zavala, Alonso A.Valenzuela, Jesus G.Sotelo Mundo, Rogerio RafaelARGININE KINASEENZIMEALLLERGENTICKhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Arginine kinase (AK) is a reversible enzyme that regulates invertebrates’ phosphagenarginine phosphate levels. AK also elicits an immune response in humans, and it is a major foodallergen in crustacea and may be a target for novel antiparasitic drugs. Although AK has beenprimarily described in the shrimp, it is also present in other invertebrates, such as the brown tickRhipicephalus sanguineus (Rs), the vector for Rocky Mountain Spotted Fever. Here we report theenzymatic activity and the crystal structure of AK from Rhipicephalus sanguineus (RsAK) in an openconformation without substrate or ligands and a theoretical structure of RsAK modeled bound withthe substrate/product (Arg-ADP) in a closed conformation. The Michaelis-Menten kinetics confirmedthat RsAK is an efficient biocatalyst due to its high kcat/Km parameter. The recombinant enzymewas expressed in bacteria and purified to a 20 mg/L culture yield. AK is an essential enzyme ininvertebrates. Future work will be focused on the RsAK enzymatic inhibition that may lead to novelstrategies to control this pest, a burden to animal and human health.Fil: Gomez Yanes, Ana C.. Centro de Investigación E/alimentos y Desarrollo A.c; MéxicoFil: Moreno Cordova, Elena N.. Centro de Investigación E/alimentos y Desarrollo A.c; MéxicoFil: Garcia Orozco, Karina D.. Centro de Investigación E/alimentos y Desarrollo A.c; MéxicoFil: Laino, Aldana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Islas Osuna, Maria A.. Centro de Investigación E/alimentos y Desarrollo A.c; MéxicoFil: Lopez Zavala, Alonso A.. Universidad de Sonora; MéxicoFil: Valenzuela, Jesus G.. Universidad de Sonora; MéxicoFil: Sotelo Mundo, Rogerio Rafael. Centro de Investigación E/alimentos y Desarrollo A.c; MéxicoMDPI2022-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/240944Gomez Yanes, Ana C.; Moreno Cordova, Elena N.; Garcia Orozco, Karina D.; Laino, Aldana; Islas Osuna, Maria A.; et al.; The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst; MDPI; Catalysts; 12; 10; 10-2022; 1-132073-4344CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/catal12101178info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-29T11:46:32Zoai:ri.conicet.gov.ar:11336/240944instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-29 11:46:32.995CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst
title The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst
spellingShingle The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst
Gomez Yanes, Ana C.
ARGININE KINASE
ENZIME
ALLLERGEN
TICK
title_short The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst
title_full The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst
title_fullStr The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst
title_full_unstemmed The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst
title_sort The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst
dc.creator.none.fl_str_mv 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 Rafael
author Gomez Yanes, Ana C.
author_facet 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 Rafael
author_role author
author2 Moreno Cordova, Elena N.
Garcia Orozco, Karina D.
Laino, Aldana
Islas Osuna, Maria A.
Lopez Zavala, Alonso A.
Valenzuela, Jesus G.
Sotelo Mundo, Rogerio Rafael
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ARGININE KINASE
ENZIME
ALLLERGEN
TICK
topic ARGININE KINASE
ENZIME
ALLLERGEN
TICK
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Arginine kinase (AK) is a reversible enzyme that regulates invertebrates’ phosphagenarginine phosphate levels. AK also elicits an immune response in humans, and it is a major foodallergen in crustacea and may be a target for novel antiparasitic drugs. Although AK has beenprimarily described in the shrimp, it is also present in other invertebrates, such as the brown tickRhipicephalus sanguineus (Rs), the vector for Rocky Mountain Spotted Fever. Here we report theenzymatic activity and the crystal structure of AK from Rhipicephalus sanguineus (RsAK) in an openconformation without substrate or ligands and a theoretical structure of RsAK modeled bound withthe substrate/product (Arg-ADP) in a closed conformation. The Michaelis-Menten kinetics confirmedthat RsAK is an efficient biocatalyst due to its high kcat/Km parameter. The recombinant enzymewas expressed in bacteria and purified to a 20 mg/L culture yield. AK is an essential enzyme ininvertebrates. Future work will be focused on the RsAK enzymatic inhibition that may lead to novelstrategies to control this pest, a burden to animal and human health.
Fil: Gomez Yanes, Ana C.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Moreno Cordova, Elena N.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Garcia Orozco, Karina D.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Laino, Aldana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Islas Osuna, Maria A.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Lopez Zavala, Alonso A.. Universidad de Sonora; México
Fil: Valenzuela, Jesus G.. Universidad de Sonora; México
Fil: Sotelo Mundo, Rogerio Rafael. Centro de Investigación E/alimentos y Desarrollo A.c; México
description Arginine kinase (AK) is a reversible enzyme that regulates invertebrates’ phosphagenarginine phosphate levels. AK also elicits an immune response in humans, and it is a major foodallergen in crustacea and may be a target for novel antiparasitic drugs. Although AK has beenprimarily described in the shrimp, it is also present in other invertebrates, such as the brown tickRhipicephalus sanguineus (Rs), the vector for Rocky Mountain Spotted Fever. Here we report theenzymatic activity and the crystal structure of AK from Rhipicephalus sanguineus (RsAK) in an openconformation without substrate or ligands and a theoretical structure of RsAK modeled bound withthe substrate/product (Arg-ADP) in a closed conformation. The Michaelis-Menten kinetics confirmedthat RsAK is an efficient biocatalyst due to its high kcat/Km parameter. The recombinant enzymewas expressed in bacteria and purified to a 20 mg/L culture yield. AK is an essential enzyme ininvertebrates. Future work will be focused on the RsAK enzymatic inhibition that may lead to novelstrategies to control this pest, a burden to animal and human health.
publishDate 2022
dc.date.none.fl_str_mv 2022-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/240944
Gomez Yanes, Ana C.; Moreno Cordova, Elena N.; Garcia Orozco, Karina D.; Laino, Aldana; Islas Osuna, Maria A.; et al.; The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst; MDPI; Catalysts; 12; 10; 10-2022; 1-13
2073-4344
CONICET Digital
CONICET
url http://hdl.handle.net/11336/240944
identifier_str_mv Gomez Yanes, Ana C.; Moreno Cordova, Elena N.; Garcia Orozco, Karina D.; Laino, Aldana; Islas Osuna, Maria A.; et al.; The Arginine Kinase from the Tick Rhipicephalus sanguineus Is an Efficient Biocatalyst; MDPI; Catalysts; 12; 10; 10-2022; 1-13
2073-4344
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/catal12101178
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1847426453295071232
score 13.10058

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