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, C.A., Alonso, G.D., Torres, H.N., Flawiá, M.M.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_10665234_v49_n1_p82_Pereira
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spelling todo:paper_10665234_v49_n1_p82_Pereira2023-10-03T16:02:08Z Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids Pereira, C.A. Alonso, G.D. Torres, H.N. Flawiá, M.M. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, 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
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.
format JOUR
author Pereira, C.A.
Alonso, G.D.
Torres, H.N.
Flawiá, M.M.
author_facet Pereira, C.A.
Alonso, G.D.
Torres, H.N.
Flawiá, M.M.
author_sort Pereira, C.A.
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
url http://hdl.handle.net/20.500.12110/paper_10665234_v49_n1_p82_Pereira
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