Synthetic Inhibitors of Nucleoside Monophosphate-Kinases
A special issue of Pharmaceuticals (ISSN 1424-8247). This special issue belongs to the section "Medicinal Chemistry".
Deadline for manuscript submissions: 25 September 2024 | Viewed by 1107
Special Issue Editors
Interests: adenylate kinase; enzymatic inhibitors; antibiotic resistance; natural products
Interests: antibiotics discovery; anticancerous drugs discovery; medicinal chemistry; organic synthesis
Special Issues, Collections and Topics in MDPI journals
Interests: computational chemistry; drug discovery; medicinal chemistry
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
The scope of the new Special issue on the inhibitors of nucleoside monophosphate-kinases (NMP kinases) (EC 2.7.4.4) is motivated by the key role of NMP kinases in metabolism, cell division and other essential cellular functions. These kinases are essential enzymes that catalyse the reversible phosphorylation of nucleoside monophospates in nucleoside diphospates. ATP is the most efficient phosphate donor. The NMP kinases involved in purine metabolism are the adenylate kinase (AMP kinase) and guanilate kinase (GMP kinase); those involved in pyrimidinic metabolism are tymidilate kinase (TMP kinase), urydilate kinase (UMP kinase), and cytidilate kinase (CMP kinase); and for eucaryotes, there is the bi-functional enzyme UMP/CMP kinase. Biochemical and crystallographic studies characterize the catalytic and structural properties of many NMP kinases. The structural and catalytic differences between bacterial NMP kinases and their eukaryotic counterparts allows advancing studies on the inhibitors of these enzymes. Mutagenesis studies greatly advance the understanding of the regulation of NMP kinases by different ligands. Principally, we are interested in the connection of human adenylate kinases and their mutants with pathological conditions. There are nine isoenzymes and several subforms of adenylate kinases described in eukaryotes that differ from their bacterial counterparts. The adenylate kinases and other NMP kinases can be viable targets for new synthetic or natural compounds.
We welcome research articles and reviews that advance the knowledge about the field of inhibitors of NMP kinases.
Dr. Mihaela Ileana Ionescu
Prof. Dr. Ovidiu Oniga
Dr. Cristina Nastasă
Guest Editors
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Keywords
- nucleoside monophosphate-kinases
- adenylate kinase
- urydilate kinase
- tymidilate kinase
- guanilate kinase
- cytidilate kinase
- natural inhibitors
- enzymatic activity
- drug design
- structural studies
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