Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi
- Autores
- Pereira, Claudio Alejandro; Alonso, Guillermo Daniel; Ivaldi, María Soledad; Bouvier, León Alberto; Torres, Hector Norberto; Flawia, Mirtha Maria
- Año de publicación
- 2003
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Arginine kinase catalyzes the transphosphorylation between phosphoarginine and ADP. Phosphoarginine is involved in temporal ATP buffering and inorganic phosphate regulation. Trypanosoma cruzi arginine kinase phosphorylates only L‐arginine (specific activity 398.9 mUE‐min−1 mg−1), and is inhibited by the arginine analogs, agmatine, canavanine, nitroarginine, and homoarginine. Canavanine and homoarginine also produce a significant inhibition of the epimastigote culture growth (79.7% and 55.8%, respectively). Inhibition constants were calculated for canavanine and homoarginine (7.55 and 6.02 mM, respectively). In addition, two novel guanidino kinase activities were detected in the epimastigote soluble extract. The development of the arginine kinase inhibitors of T. cruzi could be an important feature because the phosphagens biosynthetic pathway in trypanosomatids is different from the one in their mammalian hosts.
Fil: Pereira, Claudio Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Alonso, Guillermo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Ivaldi, María Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Bouvier, León Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Torres, Hector Norberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Flawia, Mirtha Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina - Materia
-
Canavanine
Guanidino Kinase
Homoarginine
Phosphagen Kinase
Phosphoarginine - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/43567
Ver los metadatos del registro completo
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CONICET Digital (CONICET) |
spelling |
Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruziPereira, Claudio AlejandroAlonso, Guillermo DanielIvaldi, María SoledadBouvier, León AlbertoTorres, Hector NorbertoFlawia, Mirtha MariaCanavanineGuanidino KinaseHomoargininePhosphagen KinasePhosphoargininehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Arginine kinase catalyzes the transphosphorylation between phosphoarginine and ADP. Phosphoarginine is involved in temporal ATP buffering and inorganic phosphate regulation. Trypanosoma cruzi arginine kinase phosphorylates only L‐arginine (specific activity 398.9 mUE‐min−1 mg−1), and is inhibited by the arginine analogs, agmatine, canavanine, nitroarginine, and homoarginine. Canavanine and homoarginine also produce a significant inhibition of the epimastigote culture growth (79.7% and 55.8%, respectively). Inhibition constants were calculated for canavanine and homoarginine (7.55 and 6.02 mM, respectively). In addition, two novel guanidino kinase activities were detected in the epimastigote soluble extract. The development of the arginine kinase inhibitors of T. cruzi could be an important feature because the phosphagens biosynthetic pathway in trypanosomatids is different from the one in their mammalian hosts.Fil: Pereira, Claudio Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Alonso, Guillermo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Ivaldi, María Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Bouvier, León Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Torres, Hector Norberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Flawia, Mirtha Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaWiley Blackwell Publishing, Inc2003-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/43567Pereira, Claudio Alejandro; Alonso, Guillermo Daniel; Ivaldi, María Soledad; Bouvier, León Alberto; Torres, Hector Norberto; et al.; Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi; Wiley Blackwell Publishing, Inc; Journal of Eukaryotic Microbiology; 50; 2; 12-2003; 132-1341066-5234CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1550-7408.2003.tb00247.xinfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1550-7408.2003.tb00247.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:57:37Zoai:ri.conicet.gov.ar:11336/43567instacron: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:34982025-10-15 14:57:37.818CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi |
title |
Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi |
spellingShingle |
Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi Pereira, Claudio Alejandro Canavanine Guanidino Kinase Homoarginine Phosphagen Kinase Phosphoarginine |
title_short |
Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi |
title_full |
Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi |
title_fullStr |
Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi |
title_full_unstemmed |
Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi |
title_sort |
Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi |
dc.creator.none.fl_str_mv |
Pereira, Claudio Alejandro Alonso, Guillermo Daniel Ivaldi, María Soledad Bouvier, León Alberto Torres, Hector Norberto Flawia, Mirtha Maria |
author |
Pereira, Claudio Alejandro |
author_facet |
Pereira, Claudio Alejandro Alonso, Guillermo Daniel Ivaldi, María Soledad Bouvier, León Alberto Torres, Hector Norberto Flawia, Mirtha Maria |
author_role |
author |
author2 |
Alonso, Guillermo Daniel Ivaldi, María Soledad Bouvier, León Alberto Torres, Hector Norberto Flawia, Mirtha Maria |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Canavanine Guanidino Kinase Homoarginine Phosphagen Kinase Phosphoarginine |
topic |
Canavanine Guanidino Kinase Homoarginine Phosphagen Kinase Phosphoarginine |
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 catalyzes the transphosphorylation between phosphoarginine and ADP. Phosphoarginine is involved in temporal ATP buffering and inorganic phosphate regulation. Trypanosoma cruzi arginine kinase phosphorylates only L‐arginine (specific activity 398.9 mUE‐min−1 mg−1), and is inhibited by the arginine analogs, agmatine, canavanine, nitroarginine, and homoarginine. Canavanine and homoarginine also produce a significant inhibition of the epimastigote culture growth (79.7% and 55.8%, respectively). Inhibition constants were calculated for canavanine and homoarginine (7.55 and 6.02 mM, respectively). In addition, two novel guanidino kinase activities were detected in the epimastigote soluble extract. The development of the arginine kinase inhibitors of T. cruzi could be an important feature because the phosphagens biosynthetic pathway in trypanosomatids is different from the one in their mammalian hosts. Fil: Pereira, Claudio Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Alonso, Guillermo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Ivaldi, María Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Bouvier, León Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Torres, Hector Norberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Flawia, Mirtha Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina |
description |
Arginine kinase catalyzes the transphosphorylation between phosphoarginine and ADP. Phosphoarginine is involved in temporal ATP buffering and inorganic phosphate regulation. Trypanosoma cruzi arginine kinase phosphorylates only L‐arginine (specific activity 398.9 mUE‐min−1 mg−1), and is inhibited by the arginine analogs, agmatine, canavanine, nitroarginine, and homoarginine. Canavanine and homoarginine also produce a significant inhibition of the epimastigote culture growth (79.7% and 55.8%, respectively). Inhibition constants were calculated for canavanine and homoarginine (7.55 and 6.02 mM, respectively). In addition, two novel guanidino kinase activities were detected in the epimastigote soluble extract. The development of the arginine kinase inhibitors of T. cruzi could be an important feature because the phosphagens biosynthetic pathway in trypanosomatids is different from the one in their mammalian hosts. |
publishDate |
2003 |
dc.date.none.fl_str_mv |
2003-12 |
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/11336/43567 Pereira, Claudio Alejandro; Alonso, Guillermo Daniel; Ivaldi, María Soledad; Bouvier, León Alberto; Torres, Hector Norberto; et al.; Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi; Wiley Blackwell Publishing, Inc; Journal of Eukaryotic Microbiology; 50; 2; 12-2003; 132-134 1066-5234 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/43567 |
identifier_str_mv |
Pereira, Claudio Alejandro; Alonso, Guillermo Daniel; Ivaldi, María Soledad; Bouvier, León Alberto; Torres, Hector Norberto; et al.; Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi; Wiley Blackwell Publishing, Inc; Journal of Eukaryotic Microbiology; 50; 2; 12-2003; 132-134 1066-5234 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1550-7408.2003.tb00247.x info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1550-7408.2003.tb00247.x |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
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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 |
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1846083115597955072 |
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13.22299 |