The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization
- Autores
- Bontempi, Esteban; Garcia, G. A.; Buschiazzo, A.; Henriksson, J.; Pravia, Carlos; Ruiz, Andrés Mariano; Pettersson, Ulf; Pszenny, Viviana
- Año de publicación
- 2000
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Fil: Bontempi, Esteban. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Garcia, G. A. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Buschiazzo, A. Instituto de Investigaciones Biotecnológicas, Universidad Nacional de Gral. San Martín, INTI; Argentina.
Fil: Henriksson, J. Department of Medical Genetics and Pathology, Uppsala University, Suecia.
Fil: Pravia, Carlos. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Ruiz, Andrés Mariano. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Pettersson, Ulf. Department of Medical Genetics and Pathology, Uppsala University; Suecia.
Fil: Pszenny, Viviana. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
The complete sequence and genomic characterization of the tyrosine aminotransferase (TAT) gene from Trypanosoma rangeli is reported. The gene was found to be organized in a tandem multicopy gene array. A homologous mRNA species (2.5 kb) was identified in the epimastigote form of the parasite. From the deduced amino acid sequence, the gene encodes a protein of 420 amino acids with a predicted molecular mass of 46.4 kDa and a theoretical pI of 6.23. A high sequence identity was found with the Trypanosoma cruzi, human and rat enzymes. All the essential residues for TAT enzymatic activity are conserved, as well as a pyridoxal-phosphate attachment site typical of class-I aminotransferases. The recombinant enzyme was recognized by a monoclonal antibody against the T. cruzi enzyme. Additionally, the recombinant protein showed enzymatic activity when incubated with L-tyrosine and 2-oxoglutaric acid as substrates. - Fuente
- Fems Microbiology Letters, 2000, 189(2), 253-257.
- Materia
- Trypanosoma rangeli
- Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- Repositorio
- Institución
- Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
- OAI Identificador
- oai:sgc.anlis.gob.ar:123456789/495
Ver los metadatos del registro completo
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The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterizationBontempi, EstebanGarcia, G. A.Buschiazzo, A.Henriksson, J.Pravia, CarlosRuiz, Andrés MarianoPettersson, UlfPszenny, VivianaTrypanosoma rangeliFil: Bontempi, Esteban. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.Fil: Garcia, G. A. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.Fil: Buschiazzo, A. Instituto de Investigaciones Biotecnológicas, Universidad Nacional de Gral. San Martín, INTI; Argentina.Fil: Henriksson, J. Department of Medical Genetics and Pathology, Uppsala University, Suecia.Fil: Pravia, Carlos. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.Fil: Ruiz, Andrés Mariano. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.Fil: Pettersson, Ulf. Department of Medical Genetics and Pathology, Uppsala University; Suecia.Fil: Pszenny, Viviana. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.The complete sequence and genomic characterization of the tyrosine aminotransferase (TAT) gene from Trypanosoma rangeli is reported. The gene was found to be organized in a tandem multicopy gene array. A homologous mRNA species (2.5 kb) was identified in the epimastigote form of the parasite. From the deduced amino acid sequence, the gene encodes a protein of 420 amino acids with a predicted molecular mass of 46.4 kDa and a theoretical pI of 6.23. A high sequence identity was found with the Trypanosoma cruzi, human and rat enzymes. All the essential residues for TAT enzymatic activity are conserved, as well as a pyridoxal-phosphate attachment site typical of class-I aminotransferases. The recombinant enzyme was recognized by a monoclonal antibody against the T. cruzi enzyme. Additionally, the recombinant protein showed enzymatic activity when incubated with L-tyrosine and 2-oxoglutaric acid as substrates.Federation of European Microbiological Societies2000-08-15info:ar-repo/semantics/articuloinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdf1574-6968http://sgc.anlis.gob.ar/handle/123456789/49510.1111_j.1574-6968.2000.tb09239.x.Fems Microbiology Letters, 2000, 189(2), 253-257.reponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁNinstname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"instacron:ANLISFEMS microbiology lettersenginfo:eu-repo/semantics/openAccess2025-09-29T14:30:04Zoai:sgc.anlis.gob.ar:123456789/495Institucionalhttp://sgc.anlis.gob.ar/Organismo científico-tecnológicoNo correspondehttp://sgc.anlis.gob.ar/oai/biblioteca@anlis.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:a2025-09-29 14:30:04.639Sistema de Gestión del Conocimiento ANLIS MALBRÁN - Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"false |
dc.title.none.fl_str_mv |
The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization |
title |
The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization |
spellingShingle |
The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization Bontempi, Esteban Trypanosoma rangeli |
title_short |
The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization |
title_full |
The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization |
title_fullStr |
The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization |
title_full_unstemmed |
The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization |
title_sort |
The tyrosine aminotransferase from Trypanosoma rangeli: sequence and genomic characterization |
dc.creator.none.fl_str_mv |
Bontempi, Esteban Garcia, G. A. Buschiazzo, A. Henriksson, J. Pravia, Carlos Ruiz, Andrés Mariano Pettersson, Ulf Pszenny, Viviana |
author |
Bontempi, Esteban |
author_facet |
Bontempi, Esteban Garcia, G. A. Buschiazzo, A. Henriksson, J. Pravia, Carlos Ruiz, Andrés Mariano Pettersson, Ulf Pszenny, Viviana |
author_role |
author |
author2 |
Garcia, G. A. Buschiazzo, A. Henriksson, J. Pravia, Carlos Ruiz, Andrés Mariano Pettersson, Ulf Pszenny, Viviana |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
Trypanosoma rangeli |
topic |
Trypanosoma rangeli |
dc.description.none.fl_txt_mv |
Fil: Bontempi, Esteban. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina. Fil: Garcia, G. A. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina. Fil: Buschiazzo, A. Instituto de Investigaciones Biotecnológicas, Universidad Nacional de Gral. San Martín, INTI; Argentina. Fil: Henriksson, J. Department of Medical Genetics and Pathology, Uppsala University, Suecia. Fil: Pravia, Carlos. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina. Fil: Ruiz, Andrés Mariano. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina. Fil: Pettersson, Ulf. Department of Medical Genetics and Pathology, Uppsala University; Suecia. Fil: Pszenny, Viviana. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina. The complete sequence and genomic characterization of the tyrosine aminotransferase (TAT) gene from Trypanosoma rangeli is reported. The gene was found to be organized in a tandem multicopy gene array. A homologous mRNA species (2.5 kb) was identified in the epimastigote form of the parasite. From the deduced amino acid sequence, the gene encodes a protein of 420 amino acids with a predicted molecular mass of 46.4 kDa and a theoretical pI of 6.23. A high sequence identity was found with the Trypanosoma cruzi, human and rat enzymes. All the essential residues for TAT enzymatic activity are conserved, as well as a pyridoxal-phosphate attachment site typical of class-I aminotransferases. The recombinant enzyme was recognized by a monoclonal antibody against the T. cruzi enzyme. Additionally, the recombinant protein showed enzymatic activity when incubated with L-tyrosine and 2-oxoglutaric acid as substrates. |
description |
Fil: Bontempi, Esteban. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina. |
publishDate |
2000 |
dc.date.none.fl_str_mv |
2000-08-15 |
dc.type.none.fl_str_mv |
info:ar-repo/semantics/articulo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
1574-6968 http://sgc.anlis.gob.ar/handle/123456789/495 10.1111_j.1574-6968.2000.tb09239.x. |
identifier_str_mv |
1574-6968 10.1111_j.1574-6968.2000.tb09239.x. |
url |
http://sgc.anlis.gob.ar/handle/123456789/495 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
FEMS microbiology letters |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Federation of European Microbiological Societies |
publisher.none.fl_str_mv |
Federation of European Microbiological Societies |
dc.source.none.fl_str_mv |
Fems Microbiology Letters, 2000, 189(2), 253-257. reponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁN instname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán" instacron:ANLIS |
reponame_str |
Sistema de Gestión del Conocimiento ANLIS MALBRÁN |
collection |
Sistema de Gestión del Conocimiento ANLIS MALBRÁN |
instname_str |
Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán" |
instacron_str |
ANLIS |
institution |
ANLIS |
repository.name.fl_str_mv |
Sistema de Gestión del Conocimiento ANLIS MALBRÁN - Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán" |
repository.mail.fl_str_mv |
biblioteca@anlis.gov.ar |
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1844621852821946368 |
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12.559606 |