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In enzymology, a peptide-aspartate beta-dioxygenase () is an enzyme that catalyzes the chemical reaction :peptide-L-aspartate + 2-oxoglutarate + O2 peptide-3-hydroxy-L-aspartate + succinate + CO2 The 3 substrates of this enzyme are peptide-L-aspartate, 2-oxoglutarate, and O2, whereas its 3 products are peptide-3-hydroxy-L-aspartate, succinate, and CO2. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is peptide-L-aspartate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include aspartate beta-hydroxylase, and aspartylpeptide beta-dioxygenase. It employs one cofactor, iron. ==Structural studies== As of late 2007, 4 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「Peptide-aspartate beta-dioxygenase」の詳細全文を読む スポンサード リンク
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