Document Detail


Studies on the porcine liver esterase-catalyzed hydrolysis of pentaacetyl catechin and epicatechin: application to the synthesis of novel dimers and trimers.
MedLine Citation:
PMID:  18678485     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Porcine liver esterase-catalyzed hydrolysis of 3,5,7,3',4'-pentaacetylated catechin was studied. The selectivity of the enzyme in hydrolyzing the acetate moiety is time dependent. Careful control of the duration of hydrolysis makes it possible to isolate the differentially protected catechins. Similar result was also obtained in the epicatechin series. These results are important for elaboration of epicatechin or catechin into different derivatives with defined regiochemistry. These include novel dimeric and trimeric architectures.
Authors:
Amit Basak; Sanket Das; Shrabani Bisai
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-07-17
Journal Detail:
Title:  Bioorganic & medicinal chemistry letters     Volume:  18     ISSN:  1464-3405     ISO Abbreviation:  Bioorg. Med. Chem. Lett.     Publication Date:  2008 Sep 
Date Detail:
Created Date:  2008-08-29     Completed Date:  2008-10-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9107377     Medline TA:  Bioorg Med Chem Lett     Country:  England    
Other Details:
Languages:  eng     Pagination:  4900-3     Citation Subset:  IM    
Affiliation:
Department of Chemistry, Indian Institute of Technology, IIT Road, Kharagpur, West Bengal 721 302, India.
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MeSH Terms
Descriptor/Qualifier:
Animals
Catalysis
Catechin / analogs & derivatives*,  chemical synthesis,  chemistry,  metabolism*
Dimerization
Esterases / chemistry,  metabolism*
Hydrolysis
Liver / enzymology*,  metabolism
Liver Extracts / metabolism
Swine
Chemical
Reg. No./Substance:
0/3,5,7,3',4'-Pentaacetyl catechin; 0/Liver Extracts; 154-23-4/Catechin; EC 3.1.-/Esterases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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