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In enzymology, a phosphogluconate dehydrogenase (decarboxylating) () is an enzyme that catalyzes the chemical reaction :6-phospho-D-gluconate + NADP+ D-ribulose 5-phosphate + CO2 + NADPH Thus, the two substrates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating). Other names in common use include phosphogluconic acid dehydrogenase, 6-phosphogluconic dehydrogenase, 6-phosphogluconic carboxylase, 6-phosphogluconate dehydrogenase (decarboxylating), and 6-phospho-D-gluconate dehydrogenase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, manganese. ==Enzyme Structure== The general structure, as well as several critical residues, on 6-phosphogluconate dehydrogenase appear to be well conserved over various species. The enzyme is a dimer, with each subunit containing three domains. The N-terminal coenzyme binding domain contains a Rossmann fold with additional α/β units. The second domain consists of a number of alpha helical structures, and the C-terminal domain consists of a short tail. The tails of the two subunits interact with each other to form a mobile lid on the enzyme's active site. As of late 2007, 11 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「Phosphogluconate dehydrogenase (decarboxylating)」の詳細全文を読む スポンサード リンク
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