Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites
This work contains the first description of a guanidino kinase in a flagellar unicellular parasite. The enzyme phosphorylates L-arginine and was characterized in preparations from Trypanosoma cruzi, the ethiological agent of Chagas' disease. The activity requires ATP and a divalent cation. Unde...
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2000
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v275_n2_p1495_Pereira http://hdl.handle.net/20.500.12110/paper_00219258_v275_n2_p1495_Pereira |
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paper:paper_00219258_v275_n2_p1495_Pereira2023-06-08T14:43:18Z Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites adenosine triphosphate arginine arginine kinase canavanine divalent cation guanidine derivative histidine messenger RNA phosphotransferase amino acid sequence article Chagas disease drug targeting energy transfer enzyme activity enzyme analysis enzyme inhibition molecular cloning molecular weight nonhuman nucleotide sequence open reading frame priority journal protozoon Trypanosoma cruzi Amino Acid Sequence Amino Acids Animals Arginine Kinase Base Sequence Cations, Divalent Chromatography, Affinity Chromosome Mapping Cloning, Molecular Genomic Library Humans Kinetics Molecular Sequence Data Phylogeny Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Trypanosoma cruzi Arthropoda Mammalia Protozoa Trypanosoma Trypanosoma cruzi This work contains the first description of a guanidino kinase in a flagellar unicellular parasite. The enzyme phosphorylates L-arginine and was characterized in preparations from Trypanosoma cruzi, the ethiological agent of Chagas' disease. The activity requires ATP and a divalent cation. Under Standard assay conditions (1 mM L-arginine), the presence of 5-fold higher concentrations of canavanine or histidine produced a greater than 50% enzyme inhibition. The base sequence of this enzyme revealed an open reading frame of 357 amino acids and a molecular weight of 40,201. The amino acid sequence shows all of the characteristic consensus blocks of the ATP:guanidino phosphotransferase family and a putative 'actinin-type' actin-binding domain. The highest amino acid identities of the T. cruzi sequence, about 70%, were with arginine kinases from Arthropoda. Southern and chromosome blots revealed that the kinase is encoded by a single-copy gene. Moreover, Northern blot analysis showed an mRNA subpopulation of about 2.0 kilobases, and Western blotting of T. cruzi-soluble polypeptides revealed a 40-kDa band. The finding in the parasite of a phosphagen and its biosynthetic pathway, which are totally different from those in mammalian host tissues, points out this arginine kinase as a possible chemotherapy target for Chagas' disease. 2000 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v275_n2_p1495_Pereira http://hdl.handle.net/20.500.12110/paper_00219258_v275_n2_p1495_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 |
adenosine triphosphate arginine arginine kinase canavanine divalent cation guanidine derivative histidine messenger RNA phosphotransferase amino acid sequence article Chagas disease drug targeting energy transfer enzyme activity enzyme analysis enzyme inhibition molecular cloning molecular weight nonhuman nucleotide sequence open reading frame priority journal protozoon Trypanosoma cruzi Amino Acid Sequence Amino Acids Animals Arginine Kinase Base Sequence Cations, Divalent Chromatography, Affinity Chromosome Mapping Cloning, Molecular Genomic Library Humans Kinetics Molecular Sequence Data Phylogeny Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Trypanosoma cruzi Arthropoda Mammalia Protozoa Trypanosoma Trypanosoma cruzi |
| spellingShingle |
adenosine triphosphate arginine arginine kinase canavanine divalent cation guanidine derivative histidine messenger RNA phosphotransferase amino acid sequence article Chagas disease drug targeting energy transfer enzyme activity enzyme analysis enzyme inhibition molecular cloning molecular weight nonhuman nucleotide sequence open reading frame priority journal protozoon Trypanosoma cruzi Amino Acid Sequence Amino Acids Animals Arginine Kinase Base Sequence Cations, Divalent Chromatography, Affinity Chromosome Mapping Cloning, Molecular Genomic Library Humans Kinetics Molecular Sequence Data Phylogeny Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Trypanosoma cruzi Arthropoda Mammalia Protozoa Trypanosoma Trypanosoma cruzi Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites |
| topic_facet |
adenosine triphosphate arginine arginine kinase canavanine divalent cation guanidine derivative histidine messenger RNA phosphotransferase amino acid sequence article Chagas disease drug targeting energy transfer enzyme activity enzyme analysis enzyme inhibition molecular cloning molecular weight nonhuman nucleotide sequence open reading frame priority journal protozoon Trypanosoma cruzi Amino Acid Sequence Amino Acids Animals Arginine Kinase Base Sequence Cations, Divalent Chromatography, Affinity Chromosome Mapping Cloning, Molecular Genomic Library Humans Kinetics Molecular Sequence Data Phylogeny Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Trypanosoma cruzi Arthropoda Mammalia Protozoa Trypanosoma Trypanosoma cruzi |
| description |
This work contains the first description of a guanidino kinase in a flagellar unicellular parasite. The enzyme phosphorylates L-arginine and was characterized in preparations from Trypanosoma cruzi, the ethiological agent of Chagas' disease. The activity requires ATP and a divalent cation. Under Standard assay conditions (1 mM L-arginine), the presence of 5-fold higher concentrations of canavanine or histidine produced a greater than 50% enzyme inhibition. The base sequence of this enzyme revealed an open reading frame of 357 amino acids and a molecular weight of 40,201. The amino acid sequence shows all of the characteristic consensus blocks of the ATP:guanidino phosphotransferase family and a putative 'actinin-type' actin-binding domain. The highest amino acid identities of the T. cruzi sequence, about 70%, were with arginine kinases from Arthropoda. Southern and chromosome blots revealed that the kinase is encoded by a single-copy gene. Moreover, Northern blot analysis showed an mRNA subpopulation of about 2.0 kilobases, and Western blotting of T. cruzi-soluble polypeptides revealed a 40-kDa band. The finding in the parasite of a phosphagen and its biosynthetic pathway, which are totally different from those in mammalian host tissues, points out this arginine kinase as a possible chemotherapy target for Chagas' disease. |
| title |
Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites |
| title_short |
Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites |
| title_full |
Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites |
| title_fullStr |
Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites |
| title_full_unstemmed |
Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites |
| title_sort |
trypanosoma cruzi arginine kinase characterization and cloning. a novel energetic pathway in protozoan parasites |
| publishDate |
2000 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v275_n2_p1495_Pereira http://hdl.handle.net/20.500.12110/paper_00219258_v275_n2_p1495_Pereira |
| _version_ |
1768543116560695296 |