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...
Guardado en:
| Publicado: |
2014
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01757598_v98_n7_p3013_Medici http://hdl.handle.net/20.500.12110/paper_01757598_v98_n7_p3013_Medici |
| Aporte de: |
| id |
paper:paper_01757598_v98_n7_p3013_Medici |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_01757598_v98_n7_p3013_Medici2023-06-08T15:19:00Z A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds 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. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01757598_v98_n7_p3013_Medici 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 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. |
| 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 |
| publishDate |
2014 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01757598_v98_n7_p3013_Medici http://hdl.handle.net/20.500.12110/paper_01757598_v98_n7_p3013_Medici |
| _version_ |
1768544637539057664 |