Escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of β-glucuronides

The glycosynthase derived from E. coli β-glucuronidase catalyzes the glucuronylation of a range of primary, secondary, and aryl alcohols with moderate to excellent yields. The procedure provides an efficient, stereoselective, and scalable single-step synthesis of β-glucuronides under mild conditions...

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Main Authors: Wilkinson, Shane M., Liew, Chu W., Mackay, Joel P., Mohd. Salleh, Hamzah, Withers, Stephen G., McLeod, Malcolm D.
Format: Article
Language:English
Published: American Chemical Society 2008
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Online Access:http://irep.iium.edu.my/23428/1/Organic_letters_2008.pdf
http://irep.iium.edu.my/23428/
http://pubs.acs.org/doi/abs/10.1021/ol8002767?journalCode=orlef7
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Institution: Universiti Islam Antarabangsa Malaysia
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spelling my.iium.irep.234282021-07-01T10:19:41Z http://irep.iium.edu.my/23428/ Escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of β-glucuronides Wilkinson, Shane M. Liew, Chu W. Mackay, Joel P. Mohd. Salleh, Hamzah Withers, Stephen G. McLeod, Malcolm D. T175 Industrial research. Research and development TA164 Bioengineering TP248.13 Biotechnology The glycosynthase derived from E. coli β-glucuronidase catalyzes the glucuronylation of a range of primary, secondary, and aryl alcohols with moderate to excellent yields. The procedure provides an efficient, stereoselective, and scalable single-step synthesis of β-glucuronides under mild conditions. American Chemical Society 2008 Article PeerReviewed application/pdf en http://irep.iium.edu.my/23428/1/Organic_letters_2008.pdf Wilkinson, Shane M. and Liew, Chu W. and Mackay, Joel P. and Mohd. Salleh, Hamzah and Withers, Stephen G. and McLeod, Malcolm D. (2008) Escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of β-glucuronides. Organic Letters, 10 (8). pp. 1585-1588. ISSN 1523-7060 http://pubs.acs.org/doi/abs/10.1021/ol8002767?journalCode=orlef7 10.1021/ol8002767
institution Universiti Islam Antarabangsa Malaysia
building IIUM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider International Islamic University Malaysia
content_source IIUM Repository (IREP)
url_provider http://irep.iium.edu.my/
language English
topic T175 Industrial research. Research and development
TA164 Bioengineering
TP248.13 Biotechnology
spellingShingle T175 Industrial research. Research and development
TA164 Bioengineering
TP248.13 Biotechnology
Wilkinson, Shane M.
Liew, Chu W.
Mackay, Joel P.
Mohd. Salleh, Hamzah
Withers, Stephen G.
McLeod, Malcolm D.
Escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of β-glucuronides
description The glycosynthase derived from E. coli β-glucuronidase catalyzes the glucuronylation of a range of primary, secondary, and aryl alcohols with moderate to excellent yields. The procedure provides an efficient, stereoselective, and scalable single-step synthesis of β-glucuronides under mild conditions.
format Article
author Wilkinson, Shane M.
Liew, Chu W.
Mackay, Joel P.
Mohd. Salleh, Hamzah
Withers, Stephen G.
McLeod, Malcolm D.
author_facet Wilkinson, Shane M.
Liew, Chu W.
Mackay, Joel P.
Mohd. Salleh, Hamzah
Withers, Stephen G.
McLeod, Malcolm D.
author_sort Wilkinson, Shane M.
title Escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of β-glucuronides
title_short Escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of β-glucuronides
title_full Escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of β-glucuronides
title_fullStr Escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of β-glucuronides
title_full_unstemmed Escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of β-glucuronides
title_sort escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of β-glucuronides
publisher American Chemical Society
publishDate 2008
url http://irep.iium.edu.my/23428/1/Organic_letters_2008.pdf
http://irep.iium.edu.my/23428/
http://pubs.acs.org/doi/abs/10.1021/ol8002767?journalCode=orlef7
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