A mild and quantitative procedure for the removal of nucleoside alkoxycarbonyl groups using pig liver esterase or Candida antarctica B lipase
A set of eight mono-, di-, tri- and tetraalkoxycarbonylated nucleosides was tested in order to assess their enzymatic hydrolysis. All the alkoxycarbonyl groups of the assayed substrates, from both carbonate and carbamate functions, were quantitatively hydrolysed using pig liver esterase (PLE) at pH...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_13811177_v36_n1-6_p36_Capello |
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todo:paper_13811177_v36_n1-6_p36_Capello2023-10-03T16:11:44Z A mild and quantitative procedure for the removal of nucleoside alkoxycarbonyl groups using pig liver esterase or Candida antarctica B lipase Capello, M. González, M. Rodríguez, S.D. Iglesias, L.E. Iribarren, A.M. Carbamates Carbonates Deprotection Hydrolases Nucleosides Enzymes Hydrolysis Substrates Synthesis (chemical) Carbamates Deprotection Hydrolases Nucleosides Carbonates carbamic acid carbonic acid carbonyl derivative esterase liver enzyme nucleoside derivative triacylglycerol lipase article Candida antarctica carbonylation catalyst controlled study hydrolysis kinetics nonhuman pH measurement quantitative analysis temperature dependence Candida antarctica Sus scrofa A set of eight mono-, di-, tri- and tetraalkoxycarbonylated nucleosides was tested in order to assess their enzymatic hydrolysis. All the alkoxycarbonyl groups of the assayed substrates, from both carbonate and carbamate functions, were quantitatively hydrolysed using pig liver esterase (PLE) at pH 7 and 60°C, regardless of the nucleoside base. Quantitative full alkoxycarbonyl groups removal was also reached by Candida antarctica B lipase (CAL B) under mild conditions, but in this case, longer reaction times were required. Thus, PLE appears as an useful catalyst for the mild and quantitative deprotection of nucleoside carbonates and carbamates in the synthesis of modified nucleosides. © 2005 Elsevier B.V. All rights reserved. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13811177_v36_n1-6_p36_Capello |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Carbamates Carbonates Deprotection Hydrolases Nucleosides Enzymes Hydrolysis Substrates Synthesis (chemical) Carbamates Deprotection Hydrolases Nucleosides Carbonates carbamic acid carbonic acid carbonyl derivative esterase liver enzyme nucleoside derivative triacylglycerol lipase article Candida antarctica carbonylation catalyst controlled study hydrolysis kinetics nonhuman pH measurement quantitative analysis temperature dependence Candida antarctica Sus scrofa |
| spellingShingle |
Carbamates Carbonates Deprotection Hydrolases Nucleosides Enzymes Hydrolysis Substrates Synthesis (chemical) Carbamates Deprotection Hydrolases Nucleosides Carbonates carbamic acid carbonic acid carbonyl derivative esterase liver enzyme nucleoside derivative triacylglycerol lipase article Candida antarctica carbonylation catalyst controlled study hydrolysis kinetics nonhuman pH measurement quantitative analysis temperature dependence Candida antarctica Sus scrofa Capello, M. González, M. Rodríguez, S.D. Iglesias, L.E. Iribarren, A.M. A mild and quantitative procedure for the removal of nucleoside alkoxycarbonyl groups using pig liver esterase or Candida antarctica B lipase |
| topic_facet |
Carbamates Carbonates Deprotection Hydrolases Nucleosides Enzymes Hydrolysis Substrates Synthesis (chemical) Carbamates Deprotection Hydrolases Nucleosides Carbonates carbamic acid carbonic acid carbonyl derivative esterase liver enzyme nucleoside derivative triacylglycerol lipase article Candida antarctica carbonylation catalyst controlled study hydrolysis kinetics nonhuman pH measurement quantitative analysis temperature dependence Candida antarctica Sus scrofa |
| description |
A set of eight mono-, di-, tri- and tetraalkoxycarbonylated nucleosides was tested in order to assess their enzymatic hydrolysis. All the alkoxycarbonyl groups of the assayed substrates, from both carbonate and carbamate functions, were quantitatively hydrolysed using pig liver esterase (PLE) at pH 7 and 60°C, regardless of the nucleoside base. Quantitative full alkoxycarbonyl groups removal was also reached by Candida antarctica B lipase (CAL B) under mild conditions, but in this case, longer reaction times were required. Thus, PLE appears as an useful catalyst for the mild and quantitative deprotection of nucleoside carbonates and carbamates in the synthesis of modified nucleosides. © 2005 Elsevier B.V. All rights reserved. |
| format |
JOUR |
| author |
Capello, M. González, M. Rodríguez, S.D. Iglesias, L.E. Iribarren, A.M. |
| author_facet |
Capello, M. González, M. Rodríguez, S.D. Iglesias, L.E. Iribarren, A.M. |
| author_sort |
Capello, M. |
| title |
A mild and quantitative procedure for the removal of nucleoside alkoxycarbonyl groups using pig liver esterase or Candida antarctica B lipase |
| title_short |
A mild and quantitative procedure for the removal of nucleoside alkoxycarbonyl groups using pig liver esterase or Candida antarctica B lipase |
| title_full |
A mild and quantitative procedure for the removal of nucleoside alkoxycarbonyl groups using pig liver esterase or Candida antarctica B lipase |
| title_fullStr |
A mild and quantitative procedure for the removal of nucleoside alkoxycarbonyl groups using pig liver esterase or Candida antarctica B lipase |
| title_full_unstemmed |
A mild and quantitative procedure for the removal of nucleoside alkoxycarbonyl groups using pig liver esterase or Candida antarctica B lipase |
| title_sort |
mild and quantitative procedure for the removal of nucleoside alkoxycarbonyl groups using pig liver esterase or candida antarctica b lipase |
| url |
http://hdl.handle.net/20.500.12110/paper_13811177_v36_n1-6_p36_Capello |
| work_keys_str_mv |
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