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Catalysts
Special Issues
Enzymes in Organic Synthesis
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Enzymes in Organic Synthesis

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

Deadline for manuscript submissions: closed (15 February 2014)

Special Issue Editor

Prof. Dr. Anita Maguire

E-Mail Website
Guest Editor
Department of Chemistry, University College Cork, College Road, Cork, Ireland
Interests: synthetic and mechanistic aspects of organic chemistry (including asymmetric synthesis and development of novel synthetic methodology), medicinal chemistry and synthesis of bioactive compounds, and crystal engineering

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

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

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

Published Papers (3 papers)

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Research

1203 KiB  
Article
Enantiocomplementary Preparation of (S)- and (R)-Arylalkylcarbinols by Lipase-Catalysed Resolution and Mitsunobu Inversion: Impact of Lipase Amount
by Nassima Bouzemi, Ismahane Grib, Zahia Houiene and Louisa Aribi-Zouioueche
Catalysts 2014, 4(3), 215-225; https://doi.org/10.3390/catal4030215 - 26 Jun 2014
Cited by 15 | Viewed by 5742
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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1651 KiB  
Article
Baker’s Yeast Mediated Reduction of 2-Acetyl-3-methyl Sulfolane
by Rebecca E. Deasy, Noreen O'Riordan and Anita R. Maguire
Catalysts 2014, 4(2), 186-195; https://doi.org/10.3390/catal4020186 - 18 Jun 2014
Cited by 5 | Viewed by 13143
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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2000 KiB  
Communication
Kinetic Isotope Effect of Prostaglandin H Synthase Exhibits Inverted Temperature Dependence
by Gang Wu, Richard J. Kulmacz and Ah-Lim Tsai
Catalysts 2014, 4(2), 174-185; https://doi.org/10.3390/catal4020174 - 11 Jun 2014
Cited by 3 | Viewed by 5648
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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