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In enzymology, a nucleoside-phosphate kinase () is an enzyme that catalyzes the chemical reaction〔Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 6, Academic Press, New York, 1962, p. 139-149. 〕 :ATP + nucleoside phosphate ADP + nucleoside diphosphate Thus, the two substrates of this enzyme are ATP and nucleoside monophosphate, whereas its two products are ADP and nucleoside diphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:nucleoside-phosphate phosphotransferase. This enzyme is also called NMP-kinase, or nucleoside-monophosphate kinase. ==Structure== A number of crystal structures have been solved for this class of enzymes, revealing that they share a common ATP binding domain. This section of the enzyme is commonly referred to as the P-loop, in reference to its interaction with the phosphoryl groups on ATP. This binding domain also consists of a β sheet flanked by α helices. The () typically has the amino acid sequence of Gly-X-X-X-X-Gly-Lys. Similar sequences are found in many other nucleotide-binding proteins. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Nucleoside-phosphate kinase」の詳細全文を読む スポンサード リンク
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