Special Issue "Asymmetric and Selective Biocatalysis"

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Metal Catalysis".

Deadline for manuscript submissions: closed (31 October 2016)

Special Issue Editors

Guest Editor
Prof. Dr. Jose M. Palomo

Group of Chemical Biology and Biocatalysis, Departament of Biocatalysis, Institute of Catalysis (ICP-CSIC), Marie Curie 2, Cantoblanco, Campus UAM, 28049 Madrid, Spain
Website | E-Mail
Interests: protein chemistry; nanocatalysis; biotransformations; carbohydrate chemistry; chemical biology
Guest Editor
Prof. Dr. Cesar Mateo

Group of Chemical Processes Catalyzed by enzymes, Departament of Biocatalysis, Institute of Catalysis (ICP-CSIC), Marie Curie 2, Cantoblanco, Campus UAM, 28049 Madrid, Spain
Website | E-Mail
Interests: enzyme processes; biocatalysis; CO2 transformation; red-ox processes; enzyme immobilization

Special Issue Information

Dear Colleagues,

The preparation of pure chiral building blocks with the desired configuration is extremely important in different areas, especially in the production of pharmaceuticals. In this way, biocatalysts (cells, enzymes, catalytic antibodies, or ribozymes) represent the best alternative to the chemical processes because of the high regio- and enantio-selectivity towards different substrates at very mild conditions.

This Special Issue will be focused on innovative and novel research in “Asymmetric and Selective Biotransformations”.

Prof. Dr. Jose M. Palomo
Prof. Dr. Cesar Mateo
Guest Editors

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 papers will be 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 1300 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

  • kinetic resolutions of racemic mixtures
  • asymmetric synthesis
  • oxidations
  • reductions
  • C-C bonding formation
  • regioselectivity
  • enantioselectivity

Published Papers (9 papers)

View options order results:
result details:
Displaying articles 1-9
Export citation of selected articles as:

Research

Jump to: Review

Open AccessFeature PaperCommunication Stereoselective Chemoenzymatic Synthesis of Optically Active Aryl-Substituted Oxygen-Containing Heterocycles
Catalysts 2017, 7(2), 37; https://doi.org/10.3390/catal7020037
Received: 22 December 2016 / Revised: 16 January 2017 / Accepted: 17 January 2017 / Published: 25 January 2017
Cited by 2 | PDF Full-text (1316 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
A two-step stereoselective chemoenzymatic synthesis of optically active α-aryl-substituted oxygen heterocycles was developed, exploiting a whole-cell mediated asymmetric reduction of α-, β-, and γ-chloroalkyl arylketones followed by a stereospecific cyclization of the corresponding chlorohydrins into the target heterocycles. Among the various whole cells
[...] Read more.
A two-step stereoselective chemoenzymatic synthesis of optically active α-aryl-substituted oxygen heterocycles was developed, exploiting a whole-cell mediated asymmetric reduction of α-, β-, and γ-chloroalkyl arylketones followed by a stereospecific cyclization of the corresponding chlorohydrins into the target heterocycles. Among the various whole cells screened (baker’s yeast, Kluyveromyces marxianus CBS 6556, Saccharomyces cerevisiae CBS 7336, Lactobacillus reuteri DSM 20016), baker’s yeast was the one providing the best yields and the highest enantiomeric ratios (up to 95:5 er) in the bioreduction of the above ketones. The obtained optically active chlorohydrins could be almost quantitatively cyclized in a basic medium into the corresponding α-aryl-substituted cyclic ethers without any erosion of their enantiomeric integrity. In this respect, valuable, chiral non-racemic functionalized oxygen containing heterocycles (e.g., (S)-styrene oxide, (S)-2-phenyloxetane, (S)-2-phenyltetrahydrofuran), amenable to be further elaborated on, can be smoothly and successfully generated from their prochiral precursors. Full article
(This article belongs to the Special Issue Asymmetric and Selective Biocatalysis)
Figures

Graphical abstract

Open AccessArticle N-acetylglucosamine 2-Epimerase from Pedobacter heparinus: First Experimental Evidence of a Deprotonation/Reprotonation Mechanism
Catalysts 2016, 6(12), 212; https://doi.org/10.3390/catal6120212
Received: 26 November 2016 / Revised: 11 December 2016 / Accepted: 12 December 2016 / Published: 17 December 2016
Cited by 4 | PDF Full-text (2675 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
The control of cellular N-acetylmannosamine (ManNAc) levels has been postulated to be an effective way to modulate the decoration of cell surfaces with sialic acid. N-acetylglucosamine 2-epimerase catalyzes the interconversion of N-acetylglucosamine (GlcNAc) and ManNAc. Herein, we describe the cloning,
[...] Read more.
The control of cellular N-acetylmannosamine (ManNAc) levels has been postulated to be an effective way to modulate the decoration of cell surfaces with sialic acid. N-acetylglucosamine 2-epimerase catalyzes the interconversion of N-acetylglucosamine (GlcNAc) and ManNAc. Herein, we describe the cloning, expression, purification and biochemical characterization of an unstudied N-acetylglucosamine 2-epimerase from Pedobacter heparinus (PhGn2E). To further characterize the enzyme, several N-acylated glucosamine derivatives were chemically synthesized, and subsequently used to test the substrate specificity of PhGn2E. Furthermore, NMR studies of deuterium/hydrogen exchange at the anomeric hydroxy group and C-2 positions of the substrate in the reaction mixture confirmed for the first time the postulated epimerization reaction via ring-opening/enolate formation. Site-directed mutagenesis of key residues in the active site showed that Arg63 and Glu314 are directly involved in proton abstraction and re-incorporation onto the substrate. As all mechanistically relevant active site residues also occur in all mammalian isoforms, PhGn2E can serve as a model N-acetylglucosamine 2-epimerase for further elucidation of the active site mechanism in these enzymes. Full article
(This article belongs to the Special Issue Asymmetric and Selective Biocatalysis)
Figures

Graphical abstract

Open AccessArticle Photoassisted Oxidation of Sulfides Catalyzed by Artificial Metalloenzymes Using Water as an Oxygen Source
Catalysts 2016, 6(12), 202; https://doi.org/10.3390/catal6120202
Received: 19 October 2016 / Revised: 24 November 2016 / Accepted: 6 December 2016 / Published: 12 December 2016
Cited by 1 | PDF Full-text (1566 KB) | HTML Full-text | XML Full-text
Abstract
The Mn(TpCPP)-Xln10A artificial metalloenzyme, obtained by non-covalent insertion of Mn(III)-meso-tetrakis(p-carboxyphenyl)porphyrin [Mn(TpCPP), 1-Mn] into xylanase 10A from Streptomyces lividans (Xln10A) as a host protein, was found able to catalyze the selective photo-induced oxidation of organic substrates in the presence of [Ru
[...] Read more.
The Mn(TpCPP)-Xln10A artificial metalloenzyme, obtained by non-covalent insertion of Mn(III)-meso-tetrakis(p-carboxyphenyl)porphyrin [Mn(TpCPP), 1-Mn] into xylanase 10A from Streptomyces lividans (Xln10A) as a host protein, was found able to catalyze the selective photo-induced oxidation of organic substrates in the presence of [RuII(bpy)3]2+ as a photosensitizer and [CoIII(NH3)5Cl]2+ as a sacrificial electron acceptor, using water as oxygen atom source. Full article
(This article belongs to the Special Issue Asymmetric and Selective Biocatalysis)
Figures

Graphical abstract

Open AccessFeature PaperArticle New Tailor-Made Alkyl-Aldehyde Bifunctional Supports for Lipase Immobilization
Catalysts 2016, 6(12), 191; https://doi.org/10.3390/catal6120191
Received: 28 October 2016 / Revised: 24 November 2016 / Accepted: 27 November 2016 / Published: 30 November 2016
Cited by 4 | PDF Full-text (1643 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Immobilized and stabilized lipases are important biocatalytic tools. In this paper, different tailor-made bifunctional supports were prepared for the immobilization of a new metagenomic lipase (LipC12). The new supports contained hydrophobic groups (different alkyl groups) to promote interfacial adsorption of the lipase and
[...] Read more.
Immobilized and stabilized lipases are important biocatalytic tools. In this paper, different tailor-made bifunctional supports were prepared for the immobilization of a new metagenomic lipase (LipC12). The new supports contained hydrophobic groups (different alkyl groups) to promote interfacial adsorption of the lipase and aldehyde groups to react covalently with the amino groups of side chains of the adsorbed lipase. The best catalyst was 3.5-fold more active and 5000-fold more stable than the soluble enzyme. It was successfully used in the regioselective deacetylation of peracetylated d-glucal. The PEGylated immobilized lipase showed high regioselectivity, producing high yields of the C-3 monodeacetylated product at pH 5.0 and 4 °C. Full article
(This article belongs to the Special Issue Asymmetric and Selective Biocatalysis)
Figures

Figure 1

Open AccessArticle Mechanistic and Structural Insight to an Evolved Benzoylformate Decarboxylase with Enhanced Pyruvate Decarboxylase Activity
Catalysts 2016, 6(12), 190; https://doi.org/10.3390/catal6120190
Received: 1 November 2016 / Revised: 25 November 2016 / Accepted: 28 November 2016 / Published: 30 November 2016
PDF Full-text (2448 KB) | HTML Full-text | XML Full-text
Abstract
Benzoylformate decarboxylase (BFDC) and pyruvate decarboxylase (PDC) are thiamin diphosphate-dependent enzymes that share some structural and mechanistic similarities. Both enzymes catalyze the nonoxidative decarboxylation of 2-keto acids, yet differ considerably in their substrate specificity. In particular, the BFDC from P. putida exhibits very
[...] Read more.
Benzoylformate decarboxylase (BFDC) and pyruvate decarboxylase (PDC) are thiamin diphosphate-dependent enzymes that share some structural and mechanistic similarities. Both enzymes catalyze the nonoxidative decarboxylation of 2-keto acids, yet differ considerably in their substrate specificity. In particular, the BFDC from P. putida exhibits very limited activity with pyruvate, whereas the PDCs from S. cerevisiae or from Z. mobilis show virtually no activity with benzoylformate (phenylglyoxylate). Previously, saturation mutagenesis was used to generate the BFDC T377L/A460Y variant, which exhibited a greater than 10,000-fold increase in pyruvate/benzoylformate substrate utilization ratio compared to that of wtBFDC. Much of this change could be attributed to an improvement in the Km value for pyruvate and, concomitantly, a decrease in the kcat value for benzoylformate. However, the steady-state data did not provide any details about changes in individual catalytic steps. To gain insight into the changes in conversion rates of pyruvate and benzoylformate to acetaldehyde and benzaldehyde, respectively, by the BFDC T377L/A460Y variant, reaction intermediates of both substrates were analyzed by NMR and microscopic rate constants for the elementary catalytic steps were calculated. Herein we also report the high resolution X-ray structure of the BFDC T377L/A460Y variant, which provides context for the observed changes in substrate specificity. Full article
(This article belongs to the Special Issue Asymmetric and Selective Biocatalysis)
Figures

Graphical abstract

Open AccessArticle Efficient Production of Enantiopure d-Lysine from l-Lysine by a Two-Enzyme Cascade System
Catalysts 2016, 6(11), 168; https://doi.org/10.3390/catal6110168
Received: 24 September 2016 / Revised: 23 October 2016 / Accepted: 25 October 2016 / Published: 30 October 2016
Cited by 1 | PDF Full-text (2077 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
The microbial production of d-lysine has been of great interest as a medicinal raw material. Here, a two-step process for d-lysine production from l-lysine by the successive microbial racemization and asymmetric degradation with lysine racemase and decarboxylase was developed. The
[...] Read more.
The microbial production of d-lysine has been of great interest as a medicinal raw material. Here, a two-step process for d-lysine production from l-lysine by the successive microbial racemization and asymmetric degradation with lysine racemase and decarboxylase was developed. The whole-cell activities of engineered Escherichia coli expressing racemases from the strains Proteus mirabilis (LYR) and Lactobacillus paracasei (AAR) were first investigated comparatively. When the strain BL21-LYR with higher racemization activity was employed, l-lysine was rapidly racemized to give dl-lysine, and the d-lysine yield was approximately 48% after 0.5 h. Next, l-lysine was selectively catabolized to generate cadaverine by lysine decarboxylase. The comparative analysis of the decarboxylation activities of resting whole cells, permeabilized cells, and crude enzyme revealed that the crude enzyme was the best biocatalyst for enantiopure d-lysine production. The reaction temperature, pH, metal ion additive, and pyridoxal 5′-phosphate content of this two-step production process were subsequently optimized. Under optimal conditions, 750.7 mmol/L d-lysine was finally obtained from 1710 mmol/L l-lysine after 1 h of racemization reaction and 0.5 h of decarboxylation reaction. d-lysine yield could reach 48.8% with enantiomeric excess (ee) ≥ 99%. Full article
(This article belongs to the Special Issue Asymmetric and Selective Biocatalysis)
Figures

Graphical abstract

Open AccessFeature PaperArticle Covalent Immobilization of Candida rugosa Lipase at Alkaline pH and Their Application in the Regioselective Deprotection of Per-O-acetylated Thymidine
Catalysts 2016, 6(8), 115; https://doi.org/10.3390/catal6080115
Received: 10 June 2016 / Revised: 15 July 2016 / Accepted: 27 July 2016 / Published: 2 August 2016
Cited by 11 | PDF Full-text (3441 KB) | HTML Full-text | XML Full-text
Abstract
Lipase from Candida rugosa (CRL) was stabilized at alkaline pH to overcome the inactivation problem and was immobilized for the first time by multipoint covalent attachment on different aldehyde-activated matrices. PEG was used as a stabilizing agent on the activity of CRL. At
[...] Read more.
Lipase from Candida rugosa (CRL) was stabilized at alkaline pH to overcome the inactivation problem and was immobilized for the first time by multipoint covalent attachment on different aldehyde-activated matrices. PEG was used as a stabilizing agent on the activity of CRL. At these conditions, CRL maintained 50% activity at pH 10 after 17 h incubation in the presence of 40% (w/v) of PEG, whereas the enzyme without additive was instantaneously inactive after incubation at pH 10. Thus, this enzyme was covalently immobilized at alkaline pH on three aldehyde-activated supports: aldehyde-activated Sepharose, aldehyde-activated Lewatit105 and heterofunctional aldehyde-activated EDA-Sepharose in high overall yields. Heterogeneous stable CRL catalysts at high temperature and solvent were obtained. The aldehyde-activated Sepharose-CRL preparation maintained 70% activity at 50 °C or 30% (v/v) acetonitrile after 22 h and exhibited high regioselectivity in the deprotection process of per-O-acetylated thymidine, producing the 3′-OH-5′-OAc-thymidine in 91% yield at pH 5. Full article
(This article belongs to the Special Issue Asymmetric and Selective Biocatalysis)
Figures

Graphical abstract

Review

Jump to: Research

Open AccessReview Old Yellow Enzyme-Catalysed Asymmetric Hydrogenation: Linking Family Roots with Improved Catalysis
Catalysts 2017, 7(5), 130; https://doi.org/10.3390/catal7050130
Received: 16 March 2017 / Revised: 17 April 2017 / Accepted: 25 April 2017 / Published: 29 April 2017
Cited by 6 | PDF Full-text (5815 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Asymmetric hydrogenation of activated alkenes catalysed by ene-reductases from the old yellow enzyme family (OYEs) leading to chiral products is of potential interest for industrial processes. OYEs’ dependency on the pyridine nucleotide coenzyme can be circumvented through established artificial hydride donors such as
[...] Read more.
Asymmetric hydrogenation of activated alkenes catalysed by ene-reductases from the old yellow enzyme family (OYEs) leading to chiral products is of potential interest for industrial processes. OYEs’ dependency on the pyridine nucleotide coenzyme can be circumvented through established artificial hydride donors such as nicotinamide coenzyme biomimetics (NCBs). Several OYEs were found to exhibit higher reduction rates with NCBs. In this review, we describe a new classification of OYEs into three main classes by phylogenetic and structural analysis of characterized OYEs. The family roots are linked with their use as chiral catalysts and their mode of action with NCBs. The link between bioinformatics (sequence analysis), biochemistry (structure–function analysis), and biocatalysis (conversion, enantioselectivity and kinetics) can enable an early classification of a putative ene-reductase and therefore the indication of the binding mode of various activated alkenes. Full article
(This article belongs to the Special Issue Asymmetric and Selective Biocatalysis)
Figures

Graphical abstract

Open AccessFeature PaperReview Tandem Reactions Combining Biocatalysts and Chemical Catalysts for Asymmetric Synthesis
Catalysts 2016, 6(12), 194; https://doi.org/10.3390/catal6120194
Received: 7 November 2016 / Revised: 28 November 2016 / Accepted: 29 November 2016 / Published: 5 December 2016
Cited by 9 | PDF Full-text (6342 KB) | HTML Full-text | XML Full-text
Abstract
The application of biocatalysts in the synthesis of fine chemicals and medicinal compounds has grown significantly in recent years. Particularly, there is a growing interest in the development of one-pot tandem catalytic systems combining the reactivity of a chemical catalyst with the selectivity
[...] Read more.
The application of biocatalysts in the synthesis of fine chemicals and medicinal compounds has grown significantly in recent years. Particularly, there is a growing interest in the development of one-pot tandem catalytic systems combining the reactivity of a chemical catalyst with the selectivity engendered by the active site of an enzyme. Such tandem catalytic systems can achieve levels of chemo-, regio-, and stereo-selectivities that are unattainable with a small molecule catalyst. In addition, artificial metalloenzymes widen the range of reactivities and catalyzed reactions that are potentially employable. This review highlights some of the recent examples in the past three years that combined transition metal catalysis with enzymatic catalysis. This field is still in its infancy. However, with recent advances in protein engineering, catalyst synthesis, artificial metalloenzymes and supramolecular assembly, there is great potential to develop more sophisticated tandem chemoenzymatic processes for the synthesis of structurally complex chemicals. Full article
(This article belongs to the Special Issue Asymmetric and Selective Biocatalysis)
Figures

Figure 1

Back to Top