A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds

Autores
Médici, Rosario; Garaycoechea, Juan I.; Valino, Ana Laura; Pereira, Claudio Alejandro; Lewkowicz, Elizabeth Sandra; Iribarren, Adolfo Marcelo
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Natural and modified nucleoside-5′-monophosphates and their precursors are valuable compounds widely used in biochemical studies. Bacterial nonspecific acid phosphatases (NSAPs) are a group of enzymes involved in the hydrolysis of phosphoester bonds, and some of them exhibit phosphotransferase activity. NSAP containing Enterobacter aerogenes and Raoultella planticola whole cells were evaluated in the phosphorylation of a wide range of nucleosides and nucleoside precursors using pyrophosphate as phosphate donor. To increase the productivity of the process, we developed two genetically modified strains of Escherichia coli which overexpressed NSAPs of E. aerogenes and R. planticola. These new recombinant microorganisms (E. coli BL21 pET22b-phoEa and E. coli BL21 pET22b-phoRp) showed higher activity than the corresponding wild-type strains. Reductions in the reaction times from 21 h to 60 min, from 4 h to 15 min, and from 24 h to 40 min in cases of dihydroxyacetone, inosine, and fludarabine, respectively, were obtained.
Fil: Médici, Rosario. Delft University of Technology; Países Bajos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; Argentina
Fil: Garaycoechea, Juan I.. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; Argentina
Fil: Valino, Ana Laura. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pereira, Claudio Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Médicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Médicas; Argentina
Fil: Lewkowicz, Elizabeth Sandra. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Iribarren, Adolfo Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigación en Ingeniería Genética y Biología Molecular "Dr. Hector N. Torres". Grupo Vinculado al INGEBI- Laboratorio de Biocatálisis y Biotransformaciones - LBB - UNQUI; Argentina
Materia
Phosphorylation
Biocatalysis
Nucleosides 5 Monophosphate
Sugars
Acid Phosphatase
Sugars Phosphat
Enzymatic Phosphorylation
Fludarabine 5 Monophosphate
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/20381
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/20381
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compoundsMédici, RosarioGaraycoechea, Juan I.Valino, Ana LauraPereira, Claudio AlejandroLewkowicz, Elizabeth SandraIribarren, Adolfo MarceloPhosphorylationBiocatalysisNucleosides 5 MonophosphateSugarsAcid PhosphataseSugars PhosphatEnzymatic PhosphorylationFludarabine 5 Monophosphatehttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Natural and modified nucleoside-5′-monophosphates and their precursors are valuable compounds widely used in biochemical studies. Bacterial nonspecific acid phosphatases (NSAPs) are a group of enzymes involved in the hydrolysis of phosphoester bonds, and some of them exhibit phosphotransferase activity. NSAP containing Enterobacter aerogenes and Raoultella planticola whole cells were evaluated in the phosphorylation of a wide range of nucleosides and nucleoside precursors using pyrophosphate as phosphate donor. To increase the productivity of the process, we developed two genetically modified strains of Escherichia coli which overexpressed NSAPs of E. aerogenes and R. planticola. These new recombinant microorganisms (E. coli BL21 pET22b-phoEa and E. coli BL21 pET22b-phoRp) showed higher activity than the corresponding wild-type strains. Reductions in the reaction times from 21 h to 60 min, from 4 h to 15 min, and from 24 h to 40 min in cases of dihydroxyacetone, inosine, and fludarabine, respectively, were obtained.Fil: Médici, Rosario. Delft University of Technology; Países Bajos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; ArgentinaFil: Garaycoechea, Juan I.. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; ArgentinaFil: Valino, Ana Laura. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Pereira, Claudio Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Médicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Médicas; ArgentinaFil: Lewkowicz, Elizabeth Sandra. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Iribarren, Adolfo Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigación en Ingeniería Genética y Biología Molecular "Dr. Hector N. Torres". Grupo Vinculado al INGEBI- Laboratorio de Biocatálisis y Biotransformaciones - LBB - UNQUI; ArgentinaSpringer Heidelberg2014-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/20381Médici, Rosario; Garaycoechea, Juan I.; Valino, Ana Laura; Pereira, Claudio Alejandro; Lewkowicz, Elizabeth Sandra; et al.; A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds; Springer Heidelberg; Applied Microbiology and Biotechnology; 98; 7; 4-2014; 3013-30220175-75981432-0614CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s00253-013-5194-1info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00253-013-5194-1info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:01:15Zoai:ri.conicet.gov.ar:11336/20381instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:01:15.401CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds
title A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds
spellingShingle A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds
Médici, Rosario
Phosphorylation
Biocatalysis
Nucleosides 5 Monophosphate
Sugars
Acid Phosphatase
Sugars Phosphat
Enzymatic Phosphorylation
Fludarabine 5 Monophosphate
title_short A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds
title_full A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds
title_fullStr A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds
title_full_unstemmed A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds
title_sort A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds
dc.creator.none.fl_str_mv Médici, Rosario
Garaycoechea, Juan I.
Valino, Ana Laura
Pereira, Claudio Alejandro
Lewkowicz, Elizabeth Sandra
Iribarren, Adolfo Marcelo
author Médici, Rosario
author_facet Médici, Rosario
Garaycoechea, Juan I.
Valino, Ana Laura
Pereira, Claudio Alejandro
Lewkowicz, Elizabeth Sandra
Iribarren, Adolfo Marcelo
author_role author
author2 Garaycoechea, Juan I.
Valino, Ana Laura
Pereira, Claudio Alejandro
Lewkowicz, Elizabeth Sandra
Iribarren, Adolfo Marcelo
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Phosphorylation
Biocatalysis
Nucleosides 5 Monophosphate
Sugars
Acid Phosphatase
Sugars Phosphat
Enzymatic Phosphorylation
Fludarabine 5 Monophosphate
topic Phosphorylation
Biocatalysis
Nucleosides 5 Monophosphate
Sugars
Acid Phosphatase
Sugars Phosphat
Enzymatic Phosphorylation
Fludarabine 5 Monophosphate
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Natural and modified nucleoside-5′-monophosphates and their precursors are valuable compounds widely used in biochemical studies. Bacterial nonspecific acid phosphatases (NSAPs) are a group of enzymes involved in the hydrolysis of phosphoester bonds, and some of them exhibit phosphotransferase activity. NSAP containing Enterobacter aerogenes and Raoultella planticola whole cells were evaluated in the phosphorylation of a wide range of nucleosides and nucleoside precursors using pyrophosphate as phosphate donor. To increase the productivity of the process, we developed two genetically modified strains of Escherichia coli which overexpressed NSAPs of E. aerogenes and R. planticola. These new recombinant microorganisms (E. coli BL21 pET22b-phoEa and E. coli BL21 pET22b-phoRp) showed higher activity than the corresponding wild-type strains. Reductions in the reaction times from 21 h to 60 min, from 4 h to 15 min, and from 24 h to 40 min in cases of dihydroxyacetone, inosine, and fludarabine, respectively, were obtained.
Fil: Médici, Rosario. Delft University of Technology; Países Bajos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; Argentina
Fil: Garaycoechea, Juan I.. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; Argentina
Fil: Valino, Ana Laura. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pereira, Claudio Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Médicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Médicas; Argentina
Fil: Lewkowicz, Elizabeth Sandra. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Area Química. Laboratorio de Biotransformaciones; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Iribarren, Adolfo Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigación en Ingeniería Genética y Biología Molecular "Dr. Hector N. Torres". Grupo Vinculado al INGEBI- Laboratorio de Biocatálisis y Biotransformaciones - LBB - UNQUI; Argentina
description Natural and modified nucleoside-5′-monophosphates and their precursors are valuable compounds widely used in biochemical studies. Bacterial nonspecific acid phosphatases (NSAPs) are a group of enzymes involved in the hydrolysis of phosphoester bonds, and some of them exhibit phosphotransferase activity. NSAP containing Enterobacter aerogenes and Raoultella planticola whole cells were evaluated in the phosphorylation of a wide range of nucleosides and nucleoside precursors using pyrophosphate as phosphate donor. To increase the productivity of the process, we developed two genetically modified strains of Escherichia coli which overexpressed NSAPs of E. aerogenes and R. planticola. These new recombinant microorganisms (E. coli BL21 pET22b-phoEa and E. coli BL21 pET22b-phoRp) showed higher activity than the corresponding wild-type strains. Reductions in the reaction times from 21 h to 60 min, from 4 h to 15 min, and from 24 h to 40 min in cases of dihydroxyacetone, inosine, and fludarabine, respectively, were obtained.
publishDate 2014
dc.date.none.fl_str_mv 2014-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/20381
Médici, Rosario; Garaycoechea, Juan I.; Valino, Ana Laura; Pereira, Claudio Alejandro; Lewkowicz, Elizabeth Sandra; et al.; A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds; Springer Heidelberg; Applied Microbiology and Biotechnology; 98; 7; 4-2014; 3013-3022
0175-7598
1432-0614
CONICET Digital
CONICET
url http://hdl.handle.net/11336/20381
identifier_str_mv Médici, Rosario; Garaycoechea, Juan I.; Valino, Ana Laura; Pereira, Claudio Alejandro; Lewkowicz, Elizabeth Sandra; et al.; A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds; Springer Heidelberg; Applied Microbiology and Biotechnology; 98; 7; 4-2014; 3013-3022
0175-7598
1432-0614
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s00253-013-5194-1
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00253-013-5194-1
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Springer Heidelberg
publisher.none.fl_str_mv Springer Heidelberg
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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