Biotechnological and Biomedical Applications of Enzymes Involved in the Synthesis of Nucleosides and Nucleotides—2nd Edition
A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Enzymology".
Deadline for manuscript submissions: 20 August 2024 | Viewed by 3555
Special Issue Editor
Interests: biocatalysis; nucleoside analogues; bioinformatics; protein structure; enzyme immobilization
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
Purine and pyrimidine nucleotides are involved in a multitude of biochemical processes, but they are particularly important as building blocks for RNA and DNA synthesis. Biosynthesis of nucleotides is performed through two different metabolic routes: de novo and salvage pathways. In the de novo pathway, purine nucleotides are synthesized from simple precursors such as glycine, glutamine, or aspartate. By contrast, the salvage pathway employs nucleobases to generate the corresponding nucleoside-5´-monophosphates (NMPs). This requirement for nucleobases is satisfied by means of different endogenous and/or exogenous sources of preformed nitrogen bases. Both metabolic routes, de novo and salvage pathways, lead to the synthesis of NMPs, which are subsequently phosphorylated to obtain the corresponding nucleoside-5’-di (NMPs) and triphosphates (NTPs). Due to the importance of the enzymes involved in the synthesis of nucleosides and nucleotides, they have been extensively studied as potential targets for chemotherapy against different diseases or as important biocatalysts for the synthesis of different nucleoside and nucleotide analogs. Given this background, this Special Issue will cover the most recent and relevant findings concerning biotechnological and biomedical applications of these enzymes, including (but not limited to) (i) articles focused exclusively on the enzymatic or chemo-enzymatic synthesis of nucleic acid derivatives (NADs), (ii) articles that cover new insights into the knowledge of these enzymes, and (iii) articles focused on the use of these enzymes as therapeutic targets. Along these lines, experimental and review articles from different areas, such as microbiology, molecular biology, biochemistry, biocatalysis, enzyme technology, genomics and proteomics, bioinformatics, and protein engineering, among others, are welcome.
Dr. Jesús Fernandez Lucas
Guest Editor
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Keywords
- biotransformations
- biomedicine
- enzyme technology
- biochemistry
- organic chemistry
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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.
Title: Novel directed enzyme prodrug therapy based on 2'-deoxyribosyltransferase magnetic nanoparticles
Authors: J.Acosta, V. Pisabarro, J.C.S. dos Santos , M. Bañobre-López, J. Sanz Landaluze 4, E. Pérez, J.Fernández-Lucas
Affiliation: Applied Biotechnology Group, Biomedical Science School, Universidad Europea de Madrid, Urbanización El Bosque, Calle Tajo, s/n, 28670 Villaviciosa de Odón, Spain
Abstract: To be determined
Title: Bacterial purine nucleoside phosphorylases from mesophilic and thermophilic sources in the synthesis of natural nucleosides and their modified analogues.
Authors: Irina A. Bychek; Anastasia A. Zenchenko; Maria A. Kostromina; Marat M. Khisamov; Pavel N. Solyev; Roman S. Esipov; Sergey N. Mikhailov; Irina V. Varizhuk
Affiliation: Engelhardt Institute of Molecular Biology
Abstract: Enzymatic synthesis of nucleoside derivatives is an important alternative to multi-step chemical methods traditionally used for this purpose. Despite a number of undeniable advantages of the enzymatic approach, there is a number of factors limiting its application, such as the limited substrate specificity of enzymes, the need to work at fairly low concentrations and the physicochemical properties of substrates – for example, low solubility. The research conducted by our group is dedicated to the advantages and limitations of using purine nucleoside phosphorylases (PNPs), the main enzymes for the metabolic reutilization of purines, in the synthesis of modified nucleoside analogues. In our work, the substrate specificity of PNP from various bacterial sources (mesophilic and thermophilic) was studied, and the effect of substrate, increased temperature, and the presence of organic solvents on the conversion rate was investigated.