The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships.
On the basis of the spatial structure of ascorbate oxidase [Messerschmidt, A., Rossi, A., Ladenstein, R., Huber, R., Bolognesi, M., Gatti, G., Marchesini, A., Petruzzelli, R. & Finazzi-Agro, A. (1989) J. Mol. Biol. 206, 513-529], an alignment of the amino acid sequence of the related blue oxidases, laccase and ceruloplasmin is proposed. This strongly suggests a three-domain structure for laccase closely related to ascorbate oxidase and a six-domain structure of ceruloplasmin. These domains demonstrate homology with the small blue copper proteins. The relationships suggest that laccase, like ascorbate oxidase, has a mononuclear blue copper in domain 3 and a trinuclear copper between domain 1 and 3 and ceruloplasmin has mononuclear copper ions in domains 2, 4 and 6 and a trinuclear copper between domains 1 and 6.
Max-Planck-Institut für Biochemie, Märtinsried.
A
A
Messerschmidt
R
R
Huber
D000595:Amino Acid Sequence; D000818:Animals; D001204:Ascorbate Oxidase / Q000032:analysis* / Q000235:genetics; D001400:Azurin / Q000032:analysis* / Q000235:genetics; D001426:Bacterial Proteins / Q000032:analysis*; D002570:Ceruloplasmin / Q000032:analysis* / Q000235:genetics; D005658:Fungi; D006801:Humans; D042845:Laccase; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000032:analysis* / Q000235:genetics; D010944:Plants
D001426:Bacterial Proteins; C017079:mauC protein, Methylobacterium extorquens; D001400:Azurin; D010088:Oxidoreductases; D042845:Laccase; D001204:Ascorbate Oxidase; D002570:Ceruloplasmin