Structure and mechanism of mouse cysteine dioxygenase
作者： J. G. McCoy , L. J. Bailey , E. Bitto , C. A. Bingman , D. J. Aceti
关键词:
摘要: Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid. Deficiencies in this enzyme have been linked autoimmune diseases and neurological disorders. The x-ray crystal structure CDO from Mus musculus was solved a nominal resolution 1.75 A. sequence is 91% identical that human homolog. reveals adopts typical β-barrel fold cupin superfamily. NE2 atoms His-86, -88, -140 provide metal binding site. further revealed covalent linkage between side chains Cys-93 Tyr-157, which conserved only eukaryotic proteins. Metal analysis showed recombinant contained mixture iron, nickel, zinc, with increased iron content associated catalytic activity. Details predicted active site are used present discuss plausible mechanism action for enzyme.
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