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In enzymology, an ethylbenzene hydroxylase () is an enzyme that catalyzes the chemical reaction :ethylbenzene + H2O + acceptor (S)-1-phenylethanol + reduced acceptor The 3 substrates of this enzyme are ethylbenzene, H2O, and acceptor, whereas its two products are (S)-1-phenylethanol and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The systematic name of this enzyme class is ethylbenzene:acceptor oxidoreductase. Other names in common use include ethylbenzene dehydrogenase, and ethylbenzene:(acceptor) oxidoreductase. This enzyme participates in ethylbenzene degradation by ''Aromatoleum aromaticum'', a denitrifying bacterium related to the genera ''Azoarcus'' and ''Thauera''. It is a molybdenum enzyme belonging to the DMSO reductase family. Molybdenum enzymes are distinguished by the presence of a unique active site containing molybdenum atom, one or two molybdopterins and additional ligands (i.e. aminoacid residue of Ser, Cys, SeCys or Asp and very often oxygen Mo=O ligand). EBDH is synthesized exclusively in cells grown anaerobically on ethylbenzene and has been identified as a soluble periplasmic protein. ==Structural studies== As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code . EBDH consists of three subunits of 96, 43, and 23 kDa, and contains a molybdenum cofactor and a heme b559 cofactor linked by a linear row of five iron-sulfur clusters. 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「Ethylbenzene hydroxylase」の詳細全文を読む スポンサード リンク
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