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- W889419737 abstract "This chapter describes nucleoside diphosphokinase. The term “nucleoside diphosphokinase” (NDP kinase) is used to designate a family of relatively unspecific enzymes that catalyze the transfer of the terminal phosphate group of 5'-triphosphate nucleotides to 5'-diphosphate nucleotides. All NDP kinases that have been examined to date function through the formation of enzyme-bound high-energy phosphate intermediates. In earlier studies, a notable achievement was the crystallization of NDP kinase from Brewer's yeast. Today, the only crystalline preparations of NDP kinase available are those from yeast, although several laboratories have purified NDP kinases from various sources to apparent homogeneity. The only precise studies of the subunit structure, physicochemical properties, amino acid end groups, and composition of an NDP kinase have been performed with a crystalline yeast preparation that has been found to be a homologous hexamer with a monomer of about 17,000 daltons. A recent development of considerable importance to future studies of NDP kinases is the discovery of marked electrophoretic heterogeneity of the enzyme in a number of tissues. In this chapter, molecular and catalytic properties of NDP kinase are described in detail. The functions of this enzyme in the cell are also discussed in the chapter." @default.
- W889419737 created "2016-06-24" @default.
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- W889419737 date "1973-01-01" @default.
- W889419737 modified "2023-09-27" @default.
- W889419737 title "9 Nucleoside Diphosphokinases" @default.
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- W889419737 doi "https://doi.org/10.1016/s1874-6047(08)60069-4" @default.
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