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Enzyme-Catalyzed Reactions II
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Enzyme-Catalyzed Reactions II

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

Deadline for manuscript submissions: closed (30 April 2020) | Viewed by 6076

Special Issue Editor

Prof. Dr. Lajos Novak

E-Mail Website
Guest Editor
Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, 1111 Budapest, Szt. Geller ter 4, Hungary
Interests: organic chemistry; pharmaceutics; biochemistry; enzyme-catalyzed reactions; stereocontrol; chemical research

Special Issue Information

Dear Colleagues,

We are pleased to inform you that Molecules will launch the second part of “Enzyme-Catalyzed Reactions”.

To generate chiral molecules is essential in synthetic organic chemistry, medicinal chemistry, and drug discovery. In addition to 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 do not require protective group manipulations.

The second part of this Special Issue will offer a good possibility to illustrate asymmetric catalysis using enzymes, its application in organic synthesis, and the mechanistic principles that govern these reactions. I strongly encourage authors to submit manuscripts for this Special Issues.

Prof. Dr. Lajos Novak
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. Molecules is an international peer-reviewed open access semimonthly 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

  • Enzyme catalyzed
  • Chirality
  • Stereocontrol
  • Enantioselective resolution

Published Papers (2 papers)

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Research

18 pages, 7728 KiB  
Article
Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters
by Aleksandra Leśniarek, Anna Chojnacka, Radosław Drozd, Magdalena Szymańska and Witold Gładkowski
Molecules 2020, 25(5), 1067; https://doi.org/10.3390/molecules25051067 - 27 Feb 2020
Cited by 6 | Viewed by 2389
Abstract
The influence of buffer type, co-solvent type, and acyl chain length was investigated for the enantioselective hydrolysis of racemic 4-arylbut-3-en-2-yl esters using Lecitase™ Ultra (LU). Immobilized preparations of the Lecitase™ Ultra enzyme had significantly higher activity and enantioselectivity than the free enzyme, particularly [...] Read more.
The influence of buffer type, co-solvent type, and acyl chain length was investigated for the enantioselective hydrolysis of racemic 4-arylbut-3-en-2-yl esters using Lecitase™ Ultra (LU). Immobilized preparations of the Lecitase™ Ultra enzyme had significantly higher activity and enantioselectivity than the free enzyme, particularly for 4-phenylbut-3-en-2-yl butyrate as the substrate. Moreover, the kinetic resolution with the immobilized enzyme was achieved in a much shorter time (24–48 h). Lecitase™ Ultra, immobilized on cyanogen bromide-activated agarose, was particularly effective, producing, after 24 h of reaction time in phosphate buffer (pH 7.2) with acetone as co-solvent, both (R)-alcohols and unreacted (S)-esters with good to excellent enantiomeric excesses (ee 90–99%). These conditions and enzyme were also suitable for the kinetic separation of racemic (E)-4-phenylbut-3-en-2-yl butyrate analogs containing methyl substituents on the benzene ring (4b,4c), but they did not show any enantioselectivity toward (E)-4-(4’-methoxyphenyl)but-3-en-2-yl butyrate (4d). Full article
(This article belongs to the Special Issue Enzyme-Catalyzed Reactions II)
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17 pages, 3797 KiB  
Article
The Oligomeric State of the Plasma Membrane H+-ATPase from Kluyveromyces lactis
by Yadira G. Ruiz-Granados, Valentín De La Cruz-Torres and José G. Sampedro
Molecules 2019, 24(5), 958; https://doi.org/10.3390/molecules24050958 - 8 Mar 2019
Cited by 10 | Viewed by 3414
Abstract
The plasma membrane H+-ATPase was purified from the yeast K. lactis. The oligomeric state of the H+-ATPase is not known. Size exclusion chromatography displayed two macromolecular assembly states (MASs) of different sizes for the solubilized enzyme. Blue native [...] Read more.
The plasma membrane H+-ATPase was purified from the yeast K. lactis. The oligomeric state of the H+-ATPase is not known. Size exclusion chromatography displayed two macromolecular assembly states (MASs) of different sizes for the solubilized enzyme. Blue native electrophoresis (BN-PAGE) showed the H+-ATPase hexamer in both MASs as the sole/main oligomeric state—in the aggregated and free state. The hexameric state was confirmed in dodecyl maltoside-treated plasma membranes by Western-Blot. Tetramers, dimers, and monomers were present in negligible amounts, thus depicting the oligomerization pathway with the dimer as the oligomerization unit. H+-ATPase kinetics was cooperative (n~1.9), and importantly, in both MASs significant differences were determined in intrinsic fluorescence intensity, nucleotide affinity and Vmax; hence suggesting the large MAS as the activated state of the H+-ATPase. It is concluded that the quaternary structure of the H+-ATPase is the hexamer and that a relationship seems to exist between ATPase function and the aggregation state of the hexamer. Full article
(This article belongs to the Special Issue Enzyme-Catalyzed Reactions II)
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