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Abstract:

This work reports the characterization of an arginine kinase in the unicellular parasitic flagellate Trypanosoma brucei, the etiological agent of human sleeping sickness and Nagana in livestock. The arginine kinase activity, detected in the soluble fraction obtained from procyclic forms, had a specific activity similar to that observed in Trypanosoma cruzi, about 0.2 μmol min-1mg-1. Western blot analysis of T. brucei extracts revealed two bands of 40 and 45 kDa. The putative gene sequence of this enzyme had an open reading frame for a 356-amino acid polypeptide, one less than the equivalent enzyme of T. cruzi. The deduced amino acid sequence has an 82% identity with the arginine kinase of T. cruzi, and highest amino acid identities of both trypanosomatids sequences, about 70%, were with arginine kinases from the phylum Arthropoda. In addition, the amino acid sequence possesses the five arginine residues critical for interaction with ATP as well as two glutamic acids and one cysteine required for arginine binding. The finding in trypanosomatids of a new phosphagen biosynthetic pathway, which is not present in mammalian host tissues, suggests this enzyme as a possible target for chemotherapy.

Registro:

Documento: Artículo
Título:Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids
Autor:Pereira, C.A.; Alonso, G.D.; Torres, H.N.; Flawiá, M.M.
Filiación:Inst. Invest. Ing. Gen. Biol. Molec., Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Palabras clave:Guanidino kinase; Phosphagen kinase; Phosphoarginine; Trypanosoma brucei; Trypanosoma cruzi; enzyme; trypanosomiasis; Animalia; Arthropoda; Mammalia; Mastigophora (flagellates); Protozoa; Trypanosoma; Trypanosoma brucei; Trypanosoma brucei; Trypanosoma cruzi; Trypanosoma cruzi
Año:2002
Volumen:49
Número:1
Página de inicio:82
Página de fin:85
DOI: http://dx.doi.org/10.1111/j.1550-7408.2002.tb00346.x
Título revista:Journal of Eukaryotic Microbiology
Título revista abreviado:J. Eukaryotic Microbiol.
ISSN:10665234
CODEN:JEMIE
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v49_n1_p82_Pereira

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Citas:

---------- APA ----------
Pereira, C.A., Alonso, G.D., Torres, H.N. & Flawiá, M.M. (2002) . Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids. Journal of Eukaryotic Microbiology, 49(1), 82-85.
http://dx.doi.org/10.1111/j.1550-7408.2002.tb00346.x
---------- CHICAGO ----------
Pereira, C.A., Alonso, G.D., Torres, H.N., Flawiá, M.M. "Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids" . Journal of Eukaryotic Microbiology 49, no. 1 (2002) : 82-85.
http://dx.doi.org/10.1111/j.1550-7408.2002.tb00346.x
---------- MLA ----------
Pereira, C.A., Alonso, G.D., Torres, H.N., Flawiá, M.M. "Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids" . Journal of Eukaryotic Microbiology, vol. 49, no. 1, 2002, pp. 82-85.
http://dx.doi.org/10.1111/j.1550-7408.2002.tb00346.x
---------- VANCOUVER ----------
Pereira, C.A., Alonso, G.D., Torres, H.N., Flawiá, M.M. Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids. J. Eukaryotic Microbiol. 2002;49(1):82-85.
http://dx.doi.org/10.1111/j.1550-7408.2002.tb00346.x