Academic Journal
Identification and biochemical characterization of an ATP-dependent dihydroxyacetone kinase from Trypanosoma cruzi
| العنوان: | Identification and biochemical characterization of an ATP-dependent dihydroxyacetone kinase from Trypanosoma cruzi |
|---|---|
| المؤلفون: | Viecenz, Juan Matías, Garavaglia, Patricia Andrea, Tasso, Laura Mónica, Maidana, Cristina Graciela, Bautista Cannata, Joaquín Juan, Garcia, Gabriela Andrea |
| بيانات النشر: | Academic Press Inc Elsevier Science |
| المجموعة: | CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
| مصطلحات موضوعية: | CHAGAS DISEASE, DIHYDROXYACETONE, FAD, FMN CYCLASE, GLYCEROL, PROTOZOAN, https://purl.org/becyt/ford/1.6, https://purl.org/becyt/ford/1 |
| الوصف: | 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. ; 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 ; 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 ; 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 ; Fil: ... |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 0014-4894 1090-2449 |
| Relation: | info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0014489421001156; http://hdl.handle.net/11336/166651; 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; CONICET Digital; CONICET |
| الاتاحة: | http://hdl.handle.net/11336/166651 |
| Rights: | info:eu-repo/semantics/restrictedAccess ; https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
| رقم الانضمام: | edsbas.A9429E88 |
| قاعدة البيانات: | BASE |
| تدمد: | 00144894 10902449 |
|---|