The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin Modelling and structural relationships
- 1 January 1990
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 187 (2) , 341-352
- https://doi.org/10.1111/j.1432-1033.1990.tb15311.x
Abstract
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.This publication has 33 references indexed in Scilit:
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