Status of the cofactor identity in copper oxidative enzymes

• Published in: FEBS Letters 1991-04, Vol.282 (1), p.1-4
• Main Authors: Klinman, J.P., Dooley, D.M., Duine, J.A., Knowles, P.F., Mondovi, B., Villafranca, J.J.
• Format: Article
• Language: English
• Subjects: Amine Oxidase (Copper-Containing); Analytical, structural and metabolic biochemistry; Binding Sites; Biological and medical sciences; Coenzymes - metabolism; Copper - metabolism; Copper protein; Dihydroxyphenylalanine - analogs & derivatives; Dihydroxyphenylalanine - metabolism; dopamine beta -monooxygenase; Dopamine beta-Hydroxylase - metabolism; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; galactose oxidase; Galactose Oxidase - metabolism; Oxidoreductases; Oxidoreductases Acting on CH-NH Group Donors - metabolism; PQQ Cofactor; Pyrroloquinoline quinone; Quinolones - metabolism; reviews; Topa quinone
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(91)80431-2

Much conflicting data have appeared in the literature regarding the nature of the active site structures responsible for catalysis in three classes of copper enzymes: the copper amine oxidases, dopamine β-monooxygenase and galactose oxidase. Although pyrroloquinoline quinone has been proposed to be the active site cofactor in each instance, new findings indicate this is not the case. Instead, recently available data indicate a spectrum of strategies for substrate activation, which range from direct metal catalysis (dopamine β-monooxygenase) to the involvement of protein-derived radicals (galactose oxidase) and protein-derived quinones (copper amine oxidases).