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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todo:paper_13811177_v35_n1-3_p70_Inigo2023-10-03T16:11:44Z Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers Iñigo, S. Porro, M.T. Montserrat, J.M. Iglesias, L.E. Iribarren, A.M. Deacetylation Enzymatic alcoholysis Lipases Regioselectivity Ribosides Acetylation Alcohols Catalysis Enzymes Stereochemistry Anomers Deacetylation Enzymatic alcoholysis Regioselectivity 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 catalysis deprotection reaction diastereoisomer enzyme mechanism stereochemistry temperature sensitivity Candida antarctica 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13811177_v35_n1-3_p70_Inigo |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Deacetylation Enzymatic alcoholysis Lipases Regioselectivity Ribosides Acetylation Alcohols Catalysis Enzymes Stereochemistry Anomers Deacetylation Enzymatic alcoholysis Regioselectivity 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 catalysis deprotection reaction diastereoisomer enzyme mechanism stereochemistry temperature sensitivity Candida antarctica |
| spellingShingle |
Deacetylation Enzymatic alcoholysis Lipases Regioselectivity Ribosides Acetylation Alcohols Catalysis Enzymes Stereochemistry Anomers Deacetylation Enzymatic alcoholysis Regioselectivity 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 catalysis deprotection reaction diastereoisomer enzyme mechanism stereochemistry temperature sensitivity Candida antarctica Iñigo, S. Porro, M.T. Montserrat, J.M. Iglesias, L.E. Iribarren, A.M. 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 Deacetylation Enzymatic alcoholysis Regioselectivity 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 catalysis deprotection reaction diastereoisomer enzyme mechanism stereochemistry temperature sensitivity Candida antarctica |
| 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. |
| format |
JOUR |
| author |
Iñigo, S. Porro, M.T. Montserrat, J.M. Iglesias, L.E. Iribarren, A.M. |
| author_facet |
Iñigo, S. Porro, M.T. Montserrat, J.M. Iglesias, L.E. Iribarren, A.M. |
| author_sort |
Iñigo, S. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_13811177_v35_n1-3_p70_Inigo |
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1782023840127254528 |