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In enzymology, a polyphosphate-glucose phosphotransferase () is an enzyme that catalyzes the chemical reaction :(phosphate)n + D-glucose (phosphate)n-1 + D-glucose 6-phosphate Thus, the two substrates of this enzyme are (phosphate)n and D-glucose, whereas its two products are (phosphate)n-1 and D-glucose 6-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is polyphosphate:D-glucose 6-phosphotransferase. Other names in common use include polyphosphate glucokinase, polyphosphate-D-(+)-glucose-6-phosphotransferase, and polyphosphate-glucose 6-phosphotransferase. This enzyme participates in glycolysis / gluconeogenesis. It employs one cofactor, neutral salt. ==Structural studies== As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code . 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—glucose phosphotransferase」の詳細全文を読む スポンサード リンク
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