Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers
The anomers methyl 2,3,5-tri-O-acetyl-α-d-ribofuranoside and methyl 2,3,5-tri-O-acetyl-β-d-ribofuranoside showed a different behaviour in the Candida antarctica B lipase-catalysed alcoholysis. While the enzymatic deprotection of the former proceeded regioselectively affording methyl 2,3-di-O-acetyl-...
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ftunibueairesbd:paper:paper_13811177_v35_n1-3_p70_Inigo 2023-05-15T13:51:24+02:00 Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers 2005 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13811177_v35_n1-3_p70_Inigo https://hdl.handle.net/20.500.12110/paper_13811177_v35_n1-3_p70_Inigo unknown https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13811177_v35_n1-3_p70_Inigo http://hdl.handle.net/20.500.12110/paper_13811177_v35_n1-3_p70_Inigo Deacetylation Enzymatic alcoholysis Lipases Regioselectivity Ribosides Acetylation Alcohols Catalysis Enzymes Stereochemistry Anomers Isomers furan derivative lipase B methyl 2,3 di o acetyl alpha dextro ribofuranoside methyl 2,3,5 tri o acetyl beta dextro ribofuranoside methyl 2.3.5 tri o acetyl alpha dextro ribofuranoside methyl dextro riboside unclassified drug alcoholysis article biocatalyst Candida antarctica deprotection reaction diastereoisomer enzyme mechanism temperature sensitivity 2005 ftunibueairesbd https://doi.org/20.500.12110/paper_13811177_v35_n1-3_p70_Inigo 2023-02-16T02:09:35Z The anomers methyl 2,3,5-tri-O-acetyl-α-d-ribofuranoside and methyl 2,3,5-tri-O-acetyl-β-d-ribofuranoside showed a different behaviour in the Candida antarctica B lipase-catalysed alcoholysis. While the enzymatic deprotection of the former proceeded regioselectively affording methyl 2,3-di-O-acetyl-α-d-ribofuranoside in 81% yield in 3 h at 45°C showing no further transformation, the alcoholysis of the β-diasteromer was less selective. For this anomer, mixtures of partially acetylated products were formed, but contrasting to the α epimer, full deacetylated methyl β-d-ribofuranoside was quantitatively formed at long reaction times (5 days). © 2005 Elsevier B.V. All rights reserved. Other/Unknown Material Antarc* Antarctica Biblioteca Digital FCEN-UBA (Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires) |
institution |
Open Polar |
collection |
Biblioteca Digital FCEN-UBA (Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires) |
op_collection_id |
ftunibueairesbd |
language |
unknown |
topic |
Deacetylation Enzymatic alcoholysis Lipases Regioselectivity Ribosides Acetylation Alcohols Catalysis Enzymes Stereochemistry Anomers Isomers furan derivative lipase B methyl 2,3 di o acetyl alpha dextro ribofuranoside methyl 2,3,5 tri o acetyl beta dextro ribofuranoside methyl 2.3.5 tri o acetyl alpha dextro ribofuranoside methyl dextro riboside unclassified drug alcoholysis article biocatalyst Candida antarctica deprotection reaction diastereoisomer enzyme mechanism temperature sensitivity |
spellingShingle |
Deacetylation Enzymatic alcoholysis Lipases Regioselectivity Ribosides Acetylation Alcohols Catalysis Enzymes Stereochemistry Anomers Isomers furan derivative lipase B methyl 2,3 di o acetyl alpha dextro ribofuranoside methyl 2,3,5 tri o acetyl beta dextro ribofuranoside methyl 2.3.5 tri o acetyl alpha dextro ribofuranoside methyl dextro riboside unclassified drug alcoholysis article biocatalyst Candida antarctica deprotection reaction diastereoisomer enzyme mechanism temperature sensitivity Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers |
topic_facet |
Deacetylation Enzymatic alcoholysis Lipases Regioselectivity Ribosides Acetylation Alcohols Catalysis Enzymes Stereochemistry Anomers Isomers furan derivative lipase B methyl 2,3 di o acetyl alpha dextro ribofuranoside methyl 2,3,5 tri o acetyl beta dextro ribofuranoside methyl 2.3.5 tri o acetyl alpha dextro ribofuranoside methyl dextro riboside unclassified drug alcoholysis article biocatalyst Candida antarctica deprotection reaction diastereoisomer enzyme mechanism temperature sensitivity |
description |
The anomers methyl 2,3,5-tri-O-acetyl-α-d-ribofuranoside and methyl 2,3,5-tri-O-acetyl-β-d-ribofuranoside showed a different behaviour in the Candida antarctica B lipase-catalysed alcoholysis. While the enzymatic deprotection of the former proceeded regioselectively affording methyl 2,3-di-O-acetyl-α-d-ribofuranoside in 81% yield in 3 h at 45°C showing no further transformation, the alcoholysis of the β-diasteromer was less selective. For this anomer, mixtures of partially acetylated products were formed, but contrasting to the α epimer, full deacetylated methyl β-d-ribofuranoside was quantitatively formed at long reaction times (5 days). © 2005 Elsevier B.V. All rights reserved. |
title |
Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers |
title_short |
Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers |
title_full |
Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers |
title_fullStr |
Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers |
title_full_unstemmed |
Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers |
title_sort |
deprotection of peracetylated methyl d-ribosides through enzymatic alcoholysis: different recognition of the anomers |
publishDate |
2005 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13811177_v35_n1-3_p70_Inigo https://hdl.handle.net/20.500.12110/paper_13811177_v35_n1-3_p70_Inigo |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13811177_v35_n1-3_p70_Inigo http://hdl.handle.net/20.500.12110/paper_13811177_v35_n1-3_p70_Inigo |
op_doi |
https://doi.org/20.500.12110/paper_13811177_v35_n1-3_p70_Inigo |
_version_ |
1766255255072276480 |