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| Research Group Konrad |
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Enzyme Biochemistry
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Enzyme-catalyzed phosphoryltransfer reactions universally occur in all cells. Nucleotides are notably used to accept, store, and transfer chemical energy, and they are major regulatory factors in controlling the activity of a wide variety of enzyme systems. Deoxyribonucleoside kinases catalyze the phosphorylation of deoxyribonucleosides to the corresponding monophosphates (NMPs); thus, they play a key role in the salvage of nucleosides originating from food or intracellular breakdown of DNA. Subsequently, NMPs are converted by monophosphate kinases and diphosphate kinases into diphosphates and triphosphates, which are the precursors for DNA and RNA synthesis. Moreover, all three classes of kinases play essential roles in the phosphorylation of nucleoside analogs that are used for antiviral and anticancer therapy. We pursue the design and intracellular application of enzymes as a novel concept in chemotherapy to improve the efficacy of medicinally approved drugs by specifically enhancing critical phosphorylation steps.
As a second project, our work focuses on membrane-associated guanylate kinase-homologs (MAGUKs). These constitute a family of multidomain proteins that play a scaffolding role in the assembly of signal transduction complexes at sites of cell-cell contact such as synaptic and tight junctions. MAGUKs show intra- and intermolecular associations and may exist in open and closed conformations; these structural transitions appear to be modulated by nucleotides and calmodulin as well as by other proteins that specifically bind to individual domains. The main objective here is to define the role of PDZ, SH3, and GK domains in mediating protein-protein interactions.
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Manfred Konrad
Phone: +49 (551) 201-1706
Fax: +49 551 201-1074 |
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Email: mkonrad@gwdg.de
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© 2012, Max Planck Institute for Biophysical Chemistry, Göttingen |
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