Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids

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 speci...

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Autores principales:	Pereira, Claudio Alejandro, Alonso, Guillermo Daniel, Torres, Héctor Norberto, Flawiá, Mirtha María
Publicado:	2002
Materias:	Guanidino kinase Phosphagen kinase Phosphoarginine Trypanosoma brucei Trypanosoma cruzi enzyme trypanosomiasis Animalia Arthropoda Mammalia Mastigophora (flagellates) Protozoa Trypanosoma
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v49_n1_p82_Pereira http://hdl.handle.net/20.500.12110/paper_10665234_v49_n1_p82_Pereira
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_10665234_v49_n1_p82_Pereira
record_format	dspace
spelling	paper:paper_10665234_v49_n1_p82_Pereira2023-06-08T16:04:18Z Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids Pereira, Claudio Alejandro Alonso, Guillermo Daniel Torres, Héctor Norberto Flawiá, Mirtha María 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 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. Fil:Pereira, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Alonso, G.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Flawiá, M.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2002 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v49_n1_p82_Pereira http://hdl.handle.net/20.500.12110/paper_10665234_v49_n1_p82_Pereira
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	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
spellingShingle	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 Pereira, Claudio Alejandro Alonso, Guillermo Daniel Torres, Héctor Norberto Flawiá, Mirtha María Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids
topic_facet	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
description	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.
author	Pereira, Claudio Alejandro Alonso, Guillermo Daniel Torres, Héctor Norberto Flawiá, Mirtha María
author_facet	Pereira, Claudio Alejandro Alonso, Guillermo Daniel Torres, Héctor Norberto Flawiá, Mirtha María
author_sort	Pereira, Claudio Alejandro
title	Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids
title_short	Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids
title_full	Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids
title_fullStr	Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids
title_full_unstemmed	Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids
title_sort	arginine kinase: a common feature for management of energy reserves in african and american flagellated trypanosomatids
publishDate	2002
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v49_n1_p82_Pereira http://hdl.handle.net/20.500.12110/paper_10665234_v49_n1_p82_Pereira
work_keys_str_mv	AT pereiraclaudioalejandro argininekinaseacommonfeatureformanagementofenergyreservesinafricanandamericanflagellatedtrypanosomatids AT alonsoguillermodaniel argininekinaseacommonfeatureformanagementofenergyreservesinafricanandamericanflagellatedtrypanosomatids AT torreshectornorberto argininekinaseacommonfeatureformanagementofenergyreservesinafricanandamericanflagellatedtrypanosomatids AT flawiamirthamaria argininekinaseacommonfeatureformanagementofenergyreservesinafricanandamericanflagellatedtrypanosomatids
_version_	1768543193995935744

Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids

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