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

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 activ...

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Autores principales:	Médici, R., Garaycoechea, J.I., Valino, A.L., Pereira, C.A., Lewkowicz, E.S., Iribarren, A.M.
Formato:	JOUR
Materias:	Acid phosphatase Enzymatic phosphorylation Fludarabine-5′-monophosphate Nucleosides-5′-monophosphate Sugars phosphate Escherichia coli Phosphatases Phosphorylation Sugars Biochemical studies Comparative studies Enterobacter aerogenes Genetically modified Monophosphates Recombinant microorganism Biomolecules acid phosphatase aldehyde carbohydrate dihydroxyacetone fludarabine inosine ketone nucleoside phosphate phosphotransferase pyrophosphate recombinant DNA recombinant enzyme sugar phosphate bacteriology bacterium biochemistry comparative study enzyme activity gene expression hydrolysis recombination sugar article biocatalyst Citrobacter citrobacter amalonaticus Citrobacter koseri controlled study DNA sequence Enterobacter cloacae Klebsiella nonhuman Pectobacterium carotovorum Proteus vulgaris Providencia rettgeri Raoultella planticola reaction time reduction Serratia Bacteria (microorganisms) Acid Phosphatase Carbohydrate Metabolism Enterobacteriaceae Nucleosides Organisms, Genetically Modified Phosphotransferases Time Factors
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_01757598_v98_n7_p3013_Medici
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	todo:paper_01757598_v98_n7_p3013_Medici2023-10-03T15:07:57Z A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds Médici, R. Garaycoechea, J.I. Valino, A.L. Pereira, C.A. Lewkowicz, E.S. Iribarren, A.M. Acid phosphatase Enzymatic phosphorylation Fludarabine-5′-monophosphate Nucleosides-5′-monophosphate Sugars phosphate Escherichia coli Phosphatases Phosphorylation Sugars Acid phosphatase Biochemical studies Comparative studies Enterobacter aerogenes Enzymatic phosphorylation Genetically modified Monophosphates Recombinant microorganism Biomolecules acid phosphatase aldehyde carbohydrate dihydroxyacetone fludarabine inosine ketone nucleoside phosphate phosphotransferase pyrophosphate recombinant DNA recombinant enzyme sugar phosphate bacteriology bacterium biochemistry comparative study enzyme activity gene expression hydrolysis phosphate recombination sugar article bacterium biocatalyst Citrobacter citrobacter amalonaticus Citrobacter koseri comparative study controlled study DNA sequence Enterobacter aerogenes Enterobacter cloacae enzyme activity Escherichia coli hydrolysis Klebsiella nonhuman Pectobacterium carotovorum Proteus vulgaris Providencia rettgeri Raoultella planticola reaction time reduction Serratia Bacteria (microorganisms) Enterobacter aerogenes Escherichia coli Raoultella planticola Acid Phosphatase Carbohydrate Metabolism Enterobacteriaceae Escherichia coli Nucleosides Organisms, Genetically Modified Phosphotransferases Time Factors 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. © 2013 Springer-Verlag Berlin Heidelberg. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_01757598_v98_n7_p3013_Medici
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Acid phosphatase Enzymatic phosphorylation Fludarabine-5′-monophosphate Nucleosides-5′-monophosphate Sugars phosphate Escherichia coli Phosphatases Phosphorylation Sugars Acid phosphatase Biochemical studies Comparative studies Enterobacter aerogenes Enzymatic phosphorylation Genetically modified Monophosphates Recombinant microorganism Biomolecules acid phosphatase aldehyde carbohydrate dihydroxyacetone fludarabine inosine ketone nucleoside phosphate phosphotransferase pyrophosphate recombinant DNA recombinant enzyme sugar phosphate bacteriology bacterium biochemistry comparative study enzyme activity gene expression hydrolysis phosphate recombination sugar article bacterium biocatalyst Citrobacter citrobacter amalonaticus Citrobacter koseri comparative study controlled study DNA sequence Enterobacter aerogenes Enterobacter cloacae enzyme activity Escherichia coli hydrolysis Klebsiella nonhuman Pectobacterium carotovorum Proteus vulgaris Providencia rettgeri Raoultella planticola reaction time reduction Serratia Bacteria (microorganisms) Enterobacter aerogenes Escherichia coli Raoultella planticola Acid Phosphatase Carbohydrate Metabolism Enterobacteriaceae Escherichia coli Nucleosides Organisms, Genetically Modified Phosphotransferases Time Factors
spellingShingle	Acid phosphatase Enzymatic phosphorylation Fludarabine-5′-monophosphate Nucleosides-5′-monophosphate Sugars phosphate Escherichia coli Phosphatases Phosphorylation Sugars Acid phosphatase Biochemical studies Comparative studies Enterobacter aerogenes Enzymatic phosphorylation Genetically modified Monophosphates Recombinant microorganism Biomolecules acid phosphatase aldehyde carbohydrate dihydroxyacetone fludarabine inosine ketone nucleoside phosphate phosphotransferase pyrophosphate recombinant DNA recombinant enzyme sugar phosphate bacteriology bacterium biochemistry comparative study enzyme activity gene expression hydrolysis phosphate recombination sugar article bacterium biocatalyst Citrobacter citrobacter amalonaticus Citrobacter koseri comparative study controlled study DNA sequence Enterobacter aerogenes Enterobacter cloacae enzyme activity Escherichia coli hydrolysis Klebsiella nonhuman Pectobacterium carotovorum Proteus vulgaris Providencia rettgeri Raoultella planticola reaction time reduction Serratia Bacteria (microorganisms) Enterobacter aerogenes Escherichia coli Raoultella planticola Acid Phosphatase Carbohydrate Metabolism Enterobacteriaceae Escherichia coli Nucleosides Organisms, Genetically Modified Phosphotransferases Time Factors Médici, R. Garaycoechea, J.I. Valino, A.L. Pereira, C.A. Lewkowicz, E.S. Iribarren, A.M. A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds
topic_facet	Acid phosphatase Enzymatic phosphorylation Fludarabine-5′-monophosphate Nucleosides-5′-monophosphate Sugars phosphate Escherichia coli Phosphatases Phosphorylation Sugars Acid phosphatase Biochemical studies Comparative studies Enterobacter aerogenes Enzymatic phosphorylation Genetically modified Monophosphates Recombinant microorganism Biomolecules acid phosphatase aldehyde carbohydrate dihydroxyacetone fludarabine inosine ketone nucleoside phosphate phosphotransferase pyrophosphate recombinant DNA recombinant enzyme sugar phosphate bacteriology bacterium biochemistry comparative study enzyme activity gene expression hydrolysis phosphate recombination sugar article bacterium biocatalyst Citrobacter citrobacter amalonaticus Citrobacter koseri comparative study controlled study DNA sequence Enterobacter aerogenes Enterobacter cloacae enzyme activity Escherichia coli hydrolysis Klebsiella nonhuman Pectobacterium carotovorum Proteus vulgaris Providencia rettgeri Raoultella planticola reaction time reduction Serratia Bacteria (microorganisms) Enterobacter aerogenes Escherichia coli Raoultella planticola Acid Phosphatase Carbohydrate Metabolism Enterobacteriaceae Escherichia coli Nucleosides Organisms, Genetically Modified Phosphotransferases Time Factors
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. © 2013 Springer-Verlag Berlin Heidelberg.
format	JOUR
author	Médici, R. Garaycoechea, J.I. Valino, A.L. Pereira, C.A. Lewkowicz, E.S. Iribarren, A.M.
author_facet	Médici, R. Garaycoechea, J.I. Valino, A.L. Pereira, C.A. Lewkowicz, E.S. Iribarren, A.M.
author_sort	Médici, R.
title	A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds
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	comparative study on phosphotransferase activity of acid phosphatases from raoultella planticola and enterobacter aerogenes on nucleosides, sugars, and related compounds
url	http://hdl.handle.net/20.500.12110/paper_01757598_v98_n7_p3013_Medici
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A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds

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