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In enzymology, a glutamine-fructose-6-phosphate transaminase (isomerizing) () is an enzyme that catalyzes the chemical reaction :L-glutamine + D-fructose 6-phosphate L-glutamate + D-glucosamine 6-phosphate Thus, the two substrates of this enzyme are L-glutamine and D-fructose 6-phosphate, whereas its two products are L-glutamate and D-glucosamine 6-phosphate. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:D-fructose-6-phosphate isomerase (deaminating). Other names in common use include hexosephosphate aminotransferase, glucosamine-6-phosphate isomerase (glutamine-forming), glutamine-fructose-6-phosphate transaminase (isomerizing), D-fructose-6-phosphate amidotransferase, glucosaminephosphate isomerase, glucosamine 6-phosphate synthase, and GlcN6P synthase. This enzyme participates in glutamate metabolism and aminosugars metabolism. ==Structural studies== As of late 2007, 12 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「Glutamine—fructose-6-phosphate transaminase (isomerizing)」の詳細全文を読む スポンサード リンク
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