The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships

Eur J Biochem. 1990 Jan 26;187(2):341-52. doi: 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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Ascorbate Oxidase / analysis*
  • Ascorbate Oxidase / genetics
  • Azurin / analysis*
  • Azurin / genetics
  • Bacterial Proteins / analysis*
  • Ceruloplasmin / analysis*
  • Ceruloplasmin / genetics
  • Fungi
  • Humans
  • Laccase
  • Models, Molecular
  • Molecular Sequence Data
  • Oxidoreductases / analysis*
  • Oxidoreductases / genetics
  • Plants

Substances

  • Bacterial Proteins
  • mauC protein, Methylobacterium extorquens
  • Azurin
  • Oxidoreductases
  • Laccase
  • Ascorbate Oxidase
  • Ceruloplasmin