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In enzymology, a polyphosphate kinase () is an enzyme that catalyzes the formation of polyphosphate from ATP, with chain lengths of up to a thousand or more orthophosphate molecules. :ATP + (phosphate)n ADP + (phosphate)n+1 Thus, the two substrates of this enzyme are ATP and (phosphate)n, whereas its two products are ADP and (phosphate)n+1. It is a membrane protein and goes through an intermediate stage during the reaction where it is autophosphorylated with a phosphate group covalently linked to a basic amino acid residue through an N-P bond. 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:polyphosphate phosphotransferase. This enzyme is also called polyphosphoric acid kinase. This enzyme participates in oxidative phosphorylation. ==Structural studies== As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and . 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「Polyphosphate kinase」の詳細全文を読む スポンサード リンク
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