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This brief overview describes some of the properties of various cellular phospho­transferase systems, with particular emphasis on nucleoside 5'-triphosphate (NTP)- dependent protein kinases and nucleoside kinases, for which it is widely and impli­citly assumed that ATP is the intracellular phosphate donor. Numerous examples are presented, based on the in vitro properties of these enzymes, to show that ATP is not the only, or frequently not even the major, phosphate donor, and that this is probably reflected in vivo. It is pointed out that in vitro studies of donor and acceptor speci­ficities of kinases must take account of the intracellular concentrations of nucleoside 5-triphosphates, a problem also relevant to the design of nucleoside analogues as chemotherapeutic agents. Attention is also drawn to NTP analogues as substrates/ inhibitors of protein kinases, and to several examples of low-molecular mass non- peptide substrates of these enzymes.
Protein kinase inhibitors, widely exploited for elucidation of the biological functions of kinases, have more recently come under active consideration as potential chemo­therapeutic agents for tumour and other diseases. A brief overview is presented of diverse approaches to the design and development of selective protein kinase inhi­bitors, and related problems such as donor and acceptor specificities, stereochemical aspects, emerging relationships between protein, sugar and nucleoside kinases. In particular, and contrary to popular belief that ATP-competitive inhibifcrs cannot be selective because of the close homology of the ATP catalytic sites, numerous examples are presented of such inhibitors which are both potent and selective for a given kinase or class of kinases. Some of these are undergoing preclinical trials. Attention is also directed to the role of cellular and viral protein kinases in the ljfe cycle of viruses, and the potential of these enzymes, especially those encoded by, and essential for repli­cation of, a given virus as targets for antiviral chemotherapy.
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