Special Issue "Enzyme-Catalyzed Reactions"

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A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Organic Synthesis".

Deadline for manuscript submissions: 10 November 2014

Special Issue Editor

Guest Editor
Prof. Dr. Lajos Novak
Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, 1111 Budapest, Szt. Geller ter 4, Hungary
Website: http://www.och.bme.hu/org/novak.htm
E-Mail: l-novak@mail.bme.hu
Phone: +36 1 463 2207
Fax: +36 1 4633297
Interests: synthetic organic chemistry; rearrangement reactions; enzyme-catalyzed reaction, insect pheromone; insect growth regulators; lipoxygenase enzyme inhibitors; tryptamine derivatives

Special Issue Information

Dear Colleagues,

To generate chirality is essential in synthetic organic chemistry, medicinal chemistry and drug discovery. Besides conventional chemical synthetic methods, enzymes offer an excellent tool for asymmetric synthesis and enantioselective resolution. Enzyme-catalyzed reactions show excellent chemo-, region-, and stereocontrol. Furthermore, these reactions generally proceed at room temperature at pH≈ 7, in water and don’t require protecting-group manipulations. Considering the advantage of the enzyme catalyzed reactions, this technique may be widely used in chemical and biological research.

This Special Issue on enzyme-catalyzed reactions will offer a good possibility to illustrate the asymmetric catalysis with enzyme, its application in organic synthesis, and the mechanistic principles that govern these reactions. I strongly encourage authors to submit manuscripts for this Special Issue.

Dr. Lajos Novak
Guest Editor

Submission

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. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as 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 refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules 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 1800 CHF (Swiss Francs).


Keywords

  • enzymes
  • oxidoreductases
  • transferases
  • hydrolases
  • lyases
  • osomerases
  • ligases
  • immobilized enzyme
  • enzyme engineering
  • cofactors and coenzymes
  • industrial applications

Published Papers (14 papers)

by , , , , , ,  and
Molecules 2011, 16(1), 532-542; doi:10.3390/molecules16010532
Received: 16 November 2010; in revised form: 19 December 2010 / Accepted: 11 January 2011 / Published: 12 January 2011
Show/Hide Abstract | Cited by 1 | PDF Full-text (445 KB)

by
Molecules 2011, 16(4), 3128-3145; doi:10.3390/molecules16043128
Received: 11 March 2011; in revised form: 13 April 2011 / Accepted: 13 April 2011 / Published: 13 April 2011
Show/Hide Abstract | PDF Full-text (423 KB)
abstract graphic

by , ,  and
Molecules 2011, 16(7), 5896-5904; doi:10.3390/molecules16075896
Received: 29 June 2011; in revised form: 12 July 2011 / Accepted: 12 July 2011 / Published: 14 July 2011
Show/Hide Abstract | Cited by 2 | PDF Full-text (238 KB)

by , ,  and
Molecules 2011, 16(7), 5975-5988; doi:10.3390/molecules16075975
Received: 23 June 2011; Accepted: 12 July 2011 / Published: 18 July 2011
Show/Hide Abstract | Cited by 1 | PDF Full-text (549 KB)

by , ,  and
Molecules 2011, 16(7), 6041-6059; doi:10.3390/molecules16076041
Received: 24 June 2011; in revised form: 13 July 2011 / Accepted: 17 July 2011 / Published: 19 July 2011
Show/Hide Abstract | Cited by 30 | PDF Full-text (1722 KB)

by , , , , , , , , ,  and
Molecules 2011, 16(8), 6396-6407; doi:10.3390/molecules16086396
Received: 1 July 2011; in revised form: 22 July 2011 / Accepted: 25 July 2011 / Published: 28 July 2011
Show/Hide Abstract | Cited by 8 | PDF Full-text (628 KB)
abstract graphic

by , , , , , ,  and
Molecules 2011, 16(8), 6634-6644; doi:10.3390/molecules16086634
Received: 20 June 2011; in revised form: 19 July 2011 / Accepted: 19 July 2011 / Published: 5 August 2011
Show/Hide Abstract | Cited by 1 | PDF Full-text (438 KB)

by , , , ,  and
Molecules 2011, 16(8), 6747-6757; doi:10.3390/molecules16086747
Received: 4 July 2011; in revised form: 2 August 2011 / Accepted: 4 August 2011 / Published: 9 August 2011
Show/Hide Abstract | Cited by 3 | PDF Full-text (255 KB)

by  and
Molecules 2011, 16(8), 6769-6777; doi:10.3390/molecules16086769
Received: 24 June 2011; in revised form: 28 July 2011 / Accepted: 3 August 2011 / Published: 9 August 2011
Show/Hide Abstract | Cited by 2 | PDF Full-text (115 KB)

by , , , , ,  and
Molecules 2011, 16(8), 7171-7182; doi:10.3390/molecules16087171
Received: 29 June 2011; in revised form: 16 August 2011 / Accepted: 17 August 2011 / Published: 23 August 2011
Show/Hide Abstract | Cited by 5 | PDF Full-text (545 KB)

by ,  and
Molecules 2011, 16(9), 8098-8109; doi:10.3390/molecules16098098
Received: 19 August 2011; in revised form: 14 September 2011 / Accepted: 15 September 2011 / Published: 20 September 2011
Show/Hide Abstract | Cited by 1 | PDF Full-text (552 KB)
abstract graphic

by ,  and
Molecules 2011, 16(10), 8569-8589; doi:10.3390/molecules16108569
Received: 5 September 2011; in revised form: 27 September 2011 / Accepted: 30 September 2011 / Published: 12 October 2011
Show/Hide Abstract | Cited by 3 | PDF Full-text (1423 KB) | Supplementary Files
abstract graphic

by , ,  and
Molecules 2012, 17(2), 1870-1882; doi:10.3390/molecules17021870
Received: 27 October 2011; in revised form: 7 February 2012 / Accepted: 7 February 2012 / Published: 14 February 2012
Show/Hide Abstract | Cited by 1 | PDF Full-text (322 KB)
abstract graphic

by , , ,  and
Molecules 2012, 17(8), 9835-9841; doi:10.3390/molecules17089835
Received: 14 June 2012; in revised form: 1 August 2012 / Accepted: 8 August 2012 / Published: 15 August 2012
Show/Hide Abstract | Cited by 5 | PDF Full-text (213 KB) | HTML Full-text | XML Full-text | Supplementary Files

Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Type of the Paper: Review
Title: Linking Protein Motions to Enzyme Catalysis
Authors: Priyanka Narendra Singh, Don Thelma Abeysinghe, and Amnon Kohen
Affiliations: Department of Chemistry, The University of Iowa, Iowa City, IA 52242, USA
Abstract: Enzyme motions on a broad range of time scales can play an important role in various intermolecular events including substrate binding and product release in achieving the catalyzed chemical conversion. Therefore, the relationship between protein motions and the catalytic activity is of contemporary interest in enzymology. To understand the factors influencing the rates of enzyme catalyzed reactions, it has become apparent that dynamics of protein as well as its environment must be considered. The current review presents two case studies of enzymes: dihydrofolate reductase (DHFR) and thymidylate synthase (TSase), and discuss the role of protein motions in catalyzed reaction. We will discuss the use of kinetic isotope effect as an effective tool in probing such a role in the enzyme-catalyzed reactions.

Last update: 11 August 2014

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