Asymmetric aldol reactions catalyzed by the promiscuous aldo–ketoreductase enzyme

The promiscuous aldo–ketoreductase (AKR) enzyme is used as a sustainable biocatalyst for the first time to catalyze asymmetric aldol reactions in aqueous medium. The reactions between aromatic aldehydes and cyclic/acyclic ketones give the corresponding products in moderate yields and enantioselectiv...

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Main Authors: Bayat, Saadi, Abd. Malek, Emilia, Mohd Yahaya, Normi, Salleh, Abu Bakar, Tejo, Bimo Ario, Abdul Rahman, Mohd Basyaruddin
Format: Article
Language:English
Published: Elsevier 2014
Online Access:http://psasir.upm.edu.my/id/eprint/36590/1/Asymmetric%20aldol%20reactions%20catalyzed%20by%20the%20promiscuous%20aldo.pdf
http://psasir.upm.edu.my/id/eprint/36590/
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spelling my.upm.eprints.365902015-08-20T08:07:13Z http://psasir.upm.edu.my/id/eprint/36590/ Asymmetric aldol reactions catalyzed by the promiscuous aldo–ketoreductase enzyme Bayat, Saadi Abd. Malek, Emilia Mohd Yahaya, Normi Salleh, Abu Bakar Tejo, Bimo Ario Abdul Rahman, Mohd Basyaruddin The promiscuous aldo–ketoreductase (AKR) enzyme is used as a sustainable biocatalyst for the first time to catalyze asymmetric aldol reactions in aqueous medium. The reactions between aromatic aldehydes and cyclic/acyclic ketones give the corresponding products in moderate yields and enantioselectivities in the presence of water. The influence of solvents, the mole ratio of substrates, and enzyme concentration are investigated. The mechanism of the AKR1A1-catalyzed aldol reaction is also discussed. Elsevier 2014-11 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/36590/1/Asymmetric%20aldol%20reactions%20catalyzed%20by%20the%20promiscuous%20aldo.pdf Bayat, Saadi and Abd. Malek, Emilia and Mohd Yahaya, Normi and Salleh, Abu Bakar and Tejo, Bimo Ario and Abdul Rahman, Mohd Basyaruddin (2014) Asymmetric aldol reactions catalyzed by the promiscuous aldo–ketoreductase enzyme. Tetrahedron Letters, 55 (46). pp. 6303-6306. ISSN 0040-4039; ESSN: 1873-3581 10.1016/j.tetlet.2014.09.012
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description The promiscuous aldo–ketoreductase (AKR) enzyme is used as a sustainable biocatalyst for the first time to catalyze asymmetric aldol reactions in aqueous medium. The reactions between aromatic aldehydes and cyclic/acyclic ketones give the corresponding products in moderate yields and enantioselectivities in the presence of water. The influence of solvents, the mole ratio of substrates, and enzyme concentration are investigated. The mechanism of the AKR1A1-catalyzed aldol reaction is also discussed.
format Article
author Bayat, Saadi
Abd. Malek, Emilia
Mohd Yahaya, Normi
Salleh, Abu Bakar
Tejo, Bimo Ario
Abdul Rahman, Mohd Basyaruddin
spellingShingle Bayat, Saadi
Abd. Malek, Emilia
Mohd Yahaya, Normi
Salleh, Abu Bakar
Tejo, Bimo Ario
Abdul Rahman, Mohd Basyaruddin
Asymmetric aldol reactions catalyzed by the promiscuous aldo–ketoreductase enzyme
author_facet Bayat, Saadi
Abd. Malek, Emilia
Mohd Yahaya, Normi
Salleh, Abu Bakar
Tejo, Bimo Ario
Abdul Rahman, Mohd Basyaruddin
author_sort Bayat, Saadi
title Asymmetric aldol reactions catalyzed by the promiscuous aldo–ketoreductase enzyme
title_short Asymmetric aldol reactions catalyzed by the promiscuous aldo–ketoreductase enzyme
title_full Asymmetric aldol reactions catalyzed by the promiscuous aldo–ketoreductase enzyme
title_fullStr Asymmetric aldol reactions catalyzed by the promiscuous aldo–ketoreductase enzyme
title_full_unstemmed Asymmetric aldol reactions catalyzed by the promiscuous aldo–ketoreductase enzyme
title_sort asymmetric aldol reactions catalyzed by the promiscuous aldo–ketoreductase enzyme
publisher Elsevier
publishDate 2014
url http://psasir.upm.edu.my/id/eprint/36590/1/Asymmetric%20aldol%20reactions%20catalyzed%20by%20the%20promiscuous%20aldo.pdf
http://psasir.upm.edu.my/id/eprint/36590/
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