Special Issue "Enzymes in Organic Synthesis"

A special issue of Catalysts (ISSN 2073-4344).

Deadline for manuscript submissions: closed (15 February 2014).

Special Issue Editor

Guest Editor
Prof. Dr. Anita Maguire Website E-Mail
Department of Chemistry, University College Cork, College Road, Cork, Ireland

Special Issue Information

Dear Colleagues,

The art of organic synthesis rests entirely on the ability to effect transformations between compounds in a selective and effective manner with regio- and sterocontrol, in addition to chemoselectivity. Over the past two decades development of methods for asymmetric synthesis has been a major focus mainly due to the need to access and synthesise compounds destined for pharmaceutical application in enantiopure form. Use of enzymes in organic synthesis is a particularly powerful approach to effect transformations in a highly selective manner usually under mild reaction conditions. The key advantages include the excellent enantiocontrol which can be achieved in enzyme mediated transformations in addition to chemoselectivity which cannot be achieved through traditional organic reactions. Use of enzymes aligns very much with the Green Chemistry approach. Use of enzymes in organic solvents in addition to the traditional aqueous media has significant potential in organic synthesis; in addition designer enzymes complement and enhance the application of wild type enzymes providing broader substrate scope and enhanced selectivity.

Prof. Dr. Anita Maguire
Guest Editor

Manuscript Submission Information

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Keywords

  • biocatalysis
  • biotransformation
  • stereocontrol
  • asymmetric Synthesis
  • green Chemistry
  • selectivity

Published Papers (3 papers)

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Research

Open AccessArticle
Enantiocomplementary Preparation of (S)- and (R)-Arylalkylcarbinols by Lipase-Catalysed Resolution and Mitsunobu Inversion: Impact of Lipase Amount
Catalysts 2014, 4(3), 215-225; https://doi.org/10.3390/catal4030215 - 26 Jun 2014
Cited by 10
Abstract
A series of arylalkylcarbinol derivatives were deracemized through sequential combination of Candida antarctica lipase B (CAL-B) catalyzed resolution by hydrolysis and Mitsunobu stereoinversion. The (S)-acetates were obtained in 71%–99% ee and 76%–89% yields. An enantiocomplementarity was established for the hydrolysis and [...] Read more.
A series of arylalkylcarbinol derivatives were deracemized through sequential combination of Candida antarctica lipase B (CAL-B) catalyzed resolution by hydrolysis and Mitsunobu stereoinversion. The (S)-acetates were obtained in 71%–99% ee and 76%–89% yields. An enantiocomplementarity was established for the hydrolysis and acylation reactions with CAL-B lipase. Thus, the (S) and (R) enantiomers of Indan-1-yl acetate, 1,2,3,4-tetrahydro-1-naphthalenol acetate and 1-(2-naphthyl) ethyl acetate were obtained in 91%–99% ee and 76%–89% yield. Full article
(This article belongs to the Special Issue Enzymes in Organic Synthesis)
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Open AccessArticle
Baker’s Yeast Mediated Reduction of 2-Acetyl-3-methyl Sulfolane
Catalysts 2014, 4(2), 186-195; https://doi.org/10.3390/catal4020186 - 18 Jun 2014
Cited by 5
Abstract
The baker’s yeast mediated reduction of 2-acetyl-3-methyl sulfolane 1 to provide the corresponding alcohol 2 is described. Excellent efficiency and enantioselectivity (>98% ee) has been achieved under these mild environmentally benign reaction conditions. In direct contrast, the chemical reduction of 1 proceeds [...] Read more.
The baker’s yeast mediated reduction of 2-acetyl-3-methyl sulfolane 1 to provide the corresponding alcohol 2 is described. Excellent efficiency and enantioselectivity (>98% ee) has been achieved under these mild environmentally benign reaction conditions. In direct contrast, the chemical reduction of 1 proceeds with poor yield (≤25%) and diastereocontrol. Full article
(This article belongs to the Special Issue Enzymes in Organic Synthesis)
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Open AccessCommunication
Kinetic Isotope Effect of Prostaglandin H Synthase Exhibits Inverted Temperature Dependence
Catalysts 2014, 4(2), 174-185; https://doi.org/10.3390/catal4020174 - 11 Jun 2014
Cited by 2
Abstract
Conversion of arachidonic acid to prostaglandin G2/H2 catalyzed by prostaglandin H synthase (PGHS) is proposed to involve initial transfer of the C13 pro-(S) hydrogen atom from arachidonate to the Tyr385 radical in PGHS, followed by insertion of two [...] Read more.
Conversion of arachidonic acid to prostaglandin G2/H2 catalyzed by prostaglandin H synthase (PGHS) is proposed to involve initial transfer of the C13 pro-(S) hydrogen atom from arachidonate to the Tyr385 radical in PGHS, followed by insertion of two oxygen molecules and several chemical bond rearrangements. The initial hydrogen-transfer was recently concluded to be a rate-limiting step in cyclooxygenase catalysis based on the observed intrinsic deuterium kinetic isotope effect values (Dkcat). In the present study, we have found that Dkcat values of both PGHS-1 and -2 show an unusual increase with temperatures in the range of 288–310 K, exhibiting an inverted temperature dependence. The value of lnDkcat, however, decreased linearly with 1/T, consistent with a typical Arrhenius relationship. Full article
(This article belongs to the Special Issue Enzymes in Organic Synthesis)
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