INVESTIGADORES
CAMARA Maria De Los Milagros
artículos
Título:
Singular features of trypanosomatids phosphotransferases involved in cell energy management
Autor/es:
CLAUDIO AA PEREIRAA LEÓN AA BOUVIER MARÍA DE LOS MILAGROS CÁMARA AND MARIANA RR MIRANDAA
Revista:
Enzyme Research
Editorial:
SAGE-Hindawi Access to Research
Referencias:
Año: 2011 vol. 2011 p. 1 - 12
ISSN:
2090-0414
Resumen:
Trypanosomatids are responsible for economically important veterinary affections and severe human diseases. In Africa,ffections and severe human diseases. In Africa,
Trypanosoma brucei causes sleeping sickness or African trypanosomiasis, while in America, Trypanosoma cruzi is the etiological
agent of Chagas disease. These parasites have complex life cycles which involve a wide variety of environments with very
different compositions, physicochemical properties, and availability of metabolites. As the environment changes there is a need
to maintain the nucleoside homeostasis, requiring a quick and regulated response. Most of the enzymes required for energy
management are phosphotransferases. These enzymes present a nitrogenous group or a phosphate as acceptors, and the most clear
examples are arginine kinase, nucleoside diphosphate kinase, and adenylate kinase. Trypanosoma and Leishmania have the largest
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
to maintain the nucleoside homeostasis, requiring a quick and regulated response. Most of the enzymes required for energy
management are phosphotransferases. These enzymes present a nitrogenous group or a phosphate as acceptors, and the most clear
examples are arginine kinase, nucleoside diphosphate kinase, and adenylate kinase. Trypanosoma and Leishmania have the largest
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
to maintain the nucleoside homeostasis, requiring a quick and regulated response. Most of the enzymes required for energy
management are phosphotransferases. These enzymes present a nitrogenous group or a phosphate as acceptors, and the most clear
examples are arginine kinase, nucleoside diphosphate kinase, and adenylate kinase. Trypanosoma and Leishmania have the largest
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
agent of Chagas disease. These parasites have complex life cycles which involve a wide variety of environments with very
different compositions, physicochemical properties, and availability of metabolites. As the environment changes there is a need
to maintain the nucleoside homeostasis, requiring a quick and regulated response. Most of the enzymes required for energy
management are phosphotransferases. These enzymes present a nitrogenous group or a phosphate as acceptors, and the most clear
examples are arginine kinase, nucleoside diphosphate kinase, and adenylate kinase. Trypanosoma and Leishmania have the largest
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
to maintain the nucleoside homeostasis, requiring a quick and regulated response. Most of the enzymes required for energy
management are phosphotransferases. These enzymes present a nitrogenous group or a phosphate as acceptors, and the most clear
examples are arginine kinase, nucleoside diphosphate kinase, and adenylate kinase. Trypanosoma and Leishmania have the largest
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
to maintain the nucleoside homeostasis, requiring a quick and regulated response. Most of the enzymes required for energy
management are phosphotransferases. These enzymes present a nitrogenous group or a phosphate as acceptors, and the most clear
examples are arginine kinase, nucleoside diphosphate kinase, and adenylate kinase. Trypanosoma and Leishmania have the largest
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
agent of Chagas disease. These parasites have complex life cycles which involve a wide variety of environments with very
different compositions, physicochemical properties, and availability of metabolites. As the environment changes there is a need
to maintain the nucleoside homeostasis, requiring a quick and regulated response. Most of the enzymes required for energy
management are phosphotransferases. These enzymes present a nitrogenous group or a phosphate as acceptors, and the most clear
examples are arginine kinase, nucleoside diphosphate kinase, and adenylate kinase. Trypanosoma and Leishmania have the largest
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
to maintain the nucleoside homeostasis, requiring a quick and regulated response. Most of the enzymes required for energy
management are phosphotransferases. These enzymes present a nitrogenous group or a phosphate as acceptors, and the most clear
examples are arginine kinase, nucleoside diphosphate kinase, and adenylate kinase. Trypanosoma and Leishmania have the largest
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
to maintain the nucleoside homeostasis, requiring a quick and regulated response. Most of the enzymes required for energy
management are phosphotransferases. These enzymes present a nitrogenous group or a phosphate as acceptors, and the most clear
examples are arginine kinase, nucleoside diphosphate kinase, and adenylate kinase. Trypanosoma and Leishmania have the largest
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
causes sleeping sickness or African trypanosomiasis, while in America, Trypanosoma cruzi is the etiological
agent of Chagas disease. These parasites have complex life cycles which involve a wide variety of environments with very
different compositions, physicochemical properties, and availability of metabolites. As the environment changes there is a need
to maintain the nucleoside homeostasis, requiring a quick and regulated response. Most of the enzymes required for energy
management are phosphotransferases. These enzymes present a nitrogenous group or a phosphate as acceptors, and the most clear
examples are arginine kinase, nucleoside diphosphate kinase, and adenylate kinase. Trypanosoma and Leishmania have the largest
number of phosphotransferase isoforms ever found in a single cell; some of them are absent in mammals, suggesting that these
enzymes are required in many cellular compartments associated to different biological processes. The presence of such number
of phosphotransferases and the predicted subcellular localization of each isoform support the hypothesis of the existence of an
intracellular enzymatic phosphotransfer network that communicates the spatially separated intracellular ATP consumption and
production processes. All these unique features make phosphotransferases a promising start point for rational drug design for the
treatment of human trypanosomiasis.
of phosphotrans