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The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin Modelling and structural relationships
Open accessAbstract
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.
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Metadata
- Authors
- MESSERSCHMIDT, A., & HUBER, R.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1990-01
- Volume
- 187
- Issue
- 2
- Pages
- 341-352
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2027337223
- Cited by
- 437
- References
- 0
- FWCI
- 18.63
- Type
- journal article
- Language
- en
- Open access
- bronze
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