Status of the cofactor identity in copper oxidative enzymes

FEBS Letters

Mondovi, B.⁶  Villafranca, J.J.²  Duine, J.A.¹  Klinman, J.P.⁴  Dooley, D.M.⁵  Knowles, P.F.³ 

[1] Department of Microbiology and Enzymology, Delft University of Technology, Delft, The Netherlands;Department of Chemistry, Penn State University, College Park, PA, USA;Department of Biochemistry and Molecular Biology, The University of Leeds, Leeds, UK;Department of Chemistry, University of California, Berkeley, CA 94720, USA;Department of Chemistry, Amherst College, Amherst, MA 01002, USA;Department of Biochemical Sciences and C.N.R. Centre of Molecular Biology, University ‘La Sapienza’, Rome, Italy

关键词: Copper protein;    Pyrroloquinoline quinone;    Topa quinone;   

DOI  :  10.1016/0014-5793(91)80431-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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).

【 授权许可】

Unknown