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In enzymology, a 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase () is an enzyme that catalyzes the chemical reaction :2,3-dihydro-2,3-dihydroxybenzoate + NAD+ 2,3-dihydroxybenzoate + NADH + H+ Thus, the two substrates of this enzyme are 2,3-dihydro-2,3-dihydroxybenzoate and NAD+, whereas its 3 products are 2,3-dihydroxybenzoate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase. This enzyme is also called 2,3-DHB dehydrogenase. This enzyme participates in biosynthesis of siderophore group nonribosomal. == Structure == 2,3-diDHB dehydrogenase is a tetramer protein with dimension 65x69x43 Å.〔 It has a crystallographic 222 symmetry, which exhibited for other members of short-chain oxireductase (SCOR) family of enzymes.〔 The length of each monomer is 248 residues and the weight of the protein is 24647 Da. Each monomer consists of 7 beta-pleated sheets and 6 alpha helices. Although the structure of the binding protein is not clearly defined, it was proposed that the binding pocket is made out of Leu83, Met85, Arg138, Gly140, Met141, Ser176, Met181, Gln182 and Leu185. It was also speculated that Arg138 is a likely subunit that interacts with the carboxyl group of 2,3-diDHB. Since there was a strong indication of oxidation at C3 position, Ser176 and Gln182 interact with the C2-hydroxyl group in order for the stereo-selective reaction to occur.〔 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「2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase」の詳細全文を読む スポンサード リンク
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