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4-Oxalocrotonate tautomerase : ウィキペディア英語版 | 4-Oxalocrotonate tautomerase
4-Oxalocrotonate tautomerase (EC 5.3.2.-4-OT) is an enzyme that converts 2-hydroxymuconate to the αβ-unsaturated ketone, 2-oxo-3-hexenedioate. This enzyme forms part of a bacterial metabolic pathway that oxidatively catabolizes toluene, o-xylene, 3-ethyltoluene, and 1,2,4-trimethylbenzene into intermediates of the citric acid cycle. With a monomer size of just 62 amino acid residues, the 4-Oxalocrotonate tautomerase is one of the smallest enzyme subunits known. However, in solution, the enzyme forms a hexamer of six identical subunits, so the active site may be formed by amino acid residues from several subunits.〔Subramanya HS, Roper DI, Dauter Z, Dodson EJ, Davies GJ, Wilson KS, Wigley DB. Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases. (1996) Biochemistry. 35(3):792-802. (PMID 8547259 )〕 This enzyme is also unusual in that it uses a proline residue at the amino terminus as an active site residue. ==References==
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