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dc.contributor.author
Viecenz, Juan Matías
dc.contributor.author
Garavaglia, Patricia Andrea
dc.contributor.author
Tasso, Laura Mónica
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Maidana, Cristina Graciela
dc.contributor.author
Bautista Cannata, Joaquín Juan
dc.contributor.author
Garcia, Gabriela Andrea
dc.date.available
2022-08-25T18:50:41Z
dc.date.issued
2021-12
dc.identifier.citation
Viecenz, Juan Matías; Garavaglia, Patricia Andrea; Tasso, Laura Mónica; Maidana, Cristina Graciela; Bautista Cannata, Joaquín Juan; et al.; Identification and biochemical characterization of an ATP-dependent dihydroxyacetone kinase from Trypanosoma cruzi; Academic Press Inc Elsevier Science; Experimental Parasitology; 231; 12-2021; 1-8
dc.identifier.issn
0014-4894
dc.identifier.uri
http://hdl.handle.net/11336/166651
dc.description.abstract
Dihydroxyacetone (DHA) can be used as an energy source by many cell types; however, it is toxic at high concentrations. The enzyme dihydroxyacetone kinase (DAK) has shown to be involved in DHA detoxification and osmoregulation. Among protozoa of the genus Trypanosoma, T. brucei, which causes sleeping sickness, is highly sensitive to DHA and does not have orthologous genes to DAK. Conversely, T. cruzi, the etiological agent of Chagas Disease, has two putative ATP-dependent DAK (TcDAKs) sequences in its genome. Here we show that T. cruzi epimastigote lysates present a DAK specific activity of 27.1 nmol/min/mg of protein and that this form of the parasite is able to grow in the presence of 2 mM DHA. TcDAK gene was cloned and the recombinant enzyme (recTcDAK) was expressed in Escherichia coli. An anti-recTcDAK serum reacted with a protein of the expected molecular mass of 61 kDa in epimastigotes. recTcDAK presented maximal activity using Mg+2, showing a Km of 6.5 μM for DHA and a K0.5 of 124.7 μM for ATP. As it was reported for other DAKs, recTcDAK activity was inhibited by FAD with an IC50 value of 0.33 mM. In conclusion, TcDAK is the first DAK described in trypanosomatids confirming another divergent metabolism between T. brucei and T. cruzi.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Academic Press Inc Elsevier Science
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CHAGAS DISEASE
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DIHYDROXYACETONE
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FAD
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FMN CYCLASE
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GLYCEROL
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PROTOZOAN
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Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Identification and biochemical characterization of an ATP-dependent dihydroxyacetone kinase from Trypanosoma cruzi
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2022-08-25T13:45:58Z
dc.identifier.eissn
1090-2449
dc.journal.volume
231
dc.journal.pagination
1-8
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Viecenz, Juan Matías. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud “Dr. C. G. Malbrán”. Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben”; Argentina
dc.description.fil
Fil: Garavaglia, Patricia Andrea. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud “Dr. C. G. Malbrán”. Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben”; Argentina
dc.description.fil
Fil: Tasso, Laura Mónica. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud “Dr. C. G. Malbrán”. Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben”; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Maidana, Cristina Graciela. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud “Dr. C. G. Malbrán”. Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben”; Argentina
dc.description.fil
Fil: Bautista Cannata, Joaquín Juan. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
dc.description.fil
Fil: Garcia, Gabriela Andrea. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud “Dr. C. G. Malbrán”. Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben”; Argentina
dc.journal.title
Experimental Parasitology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0014489421001156
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.exppara.2021.108178
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