Enzymatic regioselective and complete deacetylation of two arabinonucleosides
Candida antarctica lipase B (CAL-B)-catalysed regioselective deacetylation of 2′,3′,5′-tri- O-acetyl-1-β- d-arabinofuranosyluracil (1) and 2′,3′,5′-tri- O-acetyl-9-β- d-arabinofuranosyladenine (2) was studied. The choice of the reaction medium allowed the regioselective formation of products bearing...
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todo:paper_13811177_v62_n3-4_p225_Sabaini2023-10-03T16:11:46Z Enzymatic regioselective and complete deacetylation of two arabinonucleosides Sabaini, M.B. Zinni, M.A. Mohorčič, M. Friedrich, J. Iribarren, A.M. Iglesias, L.E. Keratinase Lipase Nucleosides Prodrugs Regioselectivity Candida antarctica lipase B Deacetylation Degree of acetylation Hydrolases Iso-propanols Keratinase Nucleosides Paecilomyces marquandii Prodrugs Protective group Reaction medium Regio-selective Regioselective deacetylation Biomolecules Catalysis Regioselectivity Acetylation 2 propanol 2',3',5' tri o acetyl 1 beta dextro arabinofuranosyluracil 2',3',5' tri o acetyl 9 beta dextro arabinofuranosyladenine arabinonucleoside fungal enzyme hydrolase keratinase lipase B unclassified drug vidarabine article Candida antarctica catalysis controlled study deacetylation Doratomyces microsporus drug structure enzyme assay enzyme mechanism enzyme substrate fungus nonhuman paecilomyces marquandii protein hydrolysis quantitative analysis reaction time Candida antarctica Doratomyces microsporus Paecilomyces marquandii Candida antarctica lipase B (CAL-B)-catalysed regioselective deacetylation of 2′,3′,5′-tri- O-acetyl-1-β- d-arabinofuranosyluracil (1) and 2′,3′,5′-tri- O-acetyl-9-β- d-arabinofuranosyladenine (2) was studied. The choice of the reaction medium allowed the regioselective formation of products bearing different degree of acetylation: in isopropanol, CAL-B catalysed the formation of the corresponding 2′- O-acetylated arabinonucleosides, while hydrolyses afforded the 2′,3′-di- O-acetylated products. In particular, the procedure herein described allows a simple and efficient preparation of the reported vidarabine prodrug 2′,3′-di- O-acetyl-9-β- d-arabinofuranosyladenine, avoiding the utilisation of protective groups. Moreover, to achieve full deacetylation of the assayed substrates, a set of commercial hydrolases and fungal keratinases from Doratomyces microsporus (DMK) and Paecilomyces marquandii (PMK) were tested. While only PMK and DMK catalysed the quantitative complete deacetylation of 1, DMK accomplished full deacetylation of 2 in shorter time than the other assayed enzymes. © 2009 Elsevier B.V. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13811177_v62_n3-4_p225_Sabaini |
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Universidad de Buenos Aires |
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I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Keratinase Lipase Nucleosides Prodrugs Regioselectivity Candida antarctica lipase B Deacetylation Degree of acetylation Hydrolases Iso-propanols Keratinase Nucleosides Paecilomyces marquandii Prodrugs Protective group Reaction medium Regio-selective Regioselective deacetylation Biomolecules Catalysis Regioselectivity Acetylation 2 propanol 2',3',5' tri o acetyl 1 beta dextro arabinofuranosyluracil 2',3',5' tri o acetyl 9 beta dextro arabinofuranosyladenine arabinonucleoside fungal enzyme hydrolase keratinase lipase B unclassified drug vidarabine article Candida antarctica catalysis controlled study deacetylation Doratomyces microsporus drug structure enzyme assay enzyme mechanism enzyme substrate fungus nonhuman paecilomyces marquandii protein hydrolysis quantitative analysis reaction time Candida antarctica Doratomyces microsporus Paecilomyces marquandii |
| spellingShingle |
Keratinase Lipase Nucleosides Prodrugs Regioselectivity Candida antarctica lipase B Deacetylation Degree of acetylation Hydrolases Iso-propanols Keratinase Nucleosides Paecilomyces marquandii Prodrugs Protective group Reaction medium Regio-selective Regioselective deacetylation Biomolecules Catalysis Regioselectivity Acetylation 2 propanol 2',3',5' tri o acetyl 1 beta dextro arabinofuranosyluracil 2',3',5' tri o acetyl 9 beta dextro arabinofuranosyladenine arabinonucleoside fungal enzyme hydrolase keratinase lipase B unclassified drug vidarabine article Candida antarctica catalysis controlled study deacetylation Doratomyces microsporus drug structure enzyme assay enzyme mechanism enzyme substrate fungus nonhuman paecilomyces marquandii protein hydrolysis quantitative analysis reaction time Candida antarctica Doratomyces microsporus Paecilomyces marquandii Sabaini, M.B. Zinni, M.A. Mohorčič, M. Friedrich, J. Iribarren, A.M. Iglesias, L.E. Enzymatic regioselective and complete deacetylation of two arabinonucleosides |
| topic_facet |
Keratinase Lipase Nucleosides Prodrugs Regioselectivity Candida antarctica lipase B Deacetylation Degree of acetylation Hydrolases Iso-propanols Keratinase Nucleosides Paecilomyces marquandii Prodrugs Protective group Reaction medium Regio-selective Regioselective deacetylation Biomolecules Catalysis Regioselectivity Acetylation 2 propanol 2',3',5' tri o acetyl 1 beta dextro arabinofuranosyluracil 2',3',5' tri o acetyl 9 beta dextro arabinofuranosyladenine arabinonucleoside fungal enzyme hydrolase keratinase lipase B unclassified drug vidarabine article Candida antarctica catalysis controlled study deacetylation Doratomyces microsporus drug structure enzyme assay enzyme mechanism enzyme substrate fungus nonhuman paecilomyces marquandii protein hydrolysis quantitative analysis reaction time Candida antarctica Doratomyces microsporus Paecilomyces marquandii |
| description |
Candida antarctica lipase B (CAL-B)-catalysed regioselective deacetylation of 2′,3′,5′-tri- O-acetyl-1-β- d-arabinofuranosyluracil (1) and 2′,3′,5′-tri- O-acetyl-9-β- d-arabinofuranosyladenine (2) was studied. The choice of the reaction medium allowed the regioselective formation of products bearing different degree of acetylation: in isopropanol, CAL-B catalysed the formation of the corresponding 2′- O-acetylated arabinonucleosides, while hydrolyses afforded the 2′,3′-di- O-acetylated products. In particular, the procedure herein described allows a simple and efficient preparation of the reported vidarabine prodrug 2′,3′-di- O-acetyl-9-β- d-arabinofuranosyladenine, avoiding the utilisation of protective groups. Moreover, to achieve full deacetylation of the assayed substrates, a set of commercial hydrolases and fungal keratinases from Doratomyces microsporus (DMK) and Paecilomyces marquandii (PMK) were tested. While only PMK and DMK catalysed the quantitative complete deacetylation of 1, DMK accomplished full deacetylation of 2 in shorter time than the other assayed enzymes. © 2009 Elsevier B.V. |
| format |
JOUR |
| author |
Sabaini, M.B. Zinni, M.A. Mohorčič, M. Friedrich, J. Iribarren, A.M. Iglesias, L.E. |
| author_facet |
Sabaini, M.B. Zinni, M.A. Mohorčič, M. Friedrich, J. Iribarren, A.M. Iglesias, L.E. |
| author_sort |
Sabaini, M.B. |
| title |
Enzymatic regioselective and complete deacetylation of two arabinonucleosides |
| title_short |
Enzymatic regioselective and complete deacetylation of two arabinonucleosides |
| title_full |
Enzymatic regioselective and complete deacetylation of two arabinonucleosides |
| title_fullStr |
Enzymatic regioselective and complete deacetylation of two arabinonucleosides |
| title_full_unstemmed |
Enzymatic regioselective and complete deacetylation of two arabinonucleosides |
| title_sort |
enzymatic regioselective and complete deacetylation of two arabinonucleosides |
| url |
http://hdl.handle.net/20.500.12110/paper_13811177_v62_n3-4_p225_Sabaini |
| work_keys_str_mv |
AT sabainimb enzymaticregioselectiveandcompletedeacetylationoftwoarabinonucleosides AT zinnima enzymaticregioselectiveandcompletedeacetylationoftwoarabinonucleosides AT mohorcicm enzymaticregioselectiveandcompletedeacetylationoftwoarabinonucleosides AT friedrichj enzymaticregioselectiveandcompletedeacetylationoftwoarabinonucleosides AT iribarrenam enzymaticregioselectiveandcompletedeacetylationoftwoarabinonucleosides AT iglesiasle enzymaticregioselectiveandcompletedeacetylationoftwoarabinonucleosides |
| _version_ |
1782030483983433728 |