Novel types of two-domain multi-copper oxidases: possible missing links in the evolution

FEBS Lett. 2003 Oct 23;553(3):239-44. doi: 10.1016/s0014-5793(03)01000-7.

Abstract

An analysis of the genome sequence database revealed novel types of two-domain multi-copper oxidases. The two-domain proteins have the conspicuous combination of blue-copper and inter-domain trinuclear copper binding residues, which is common in ceruloplasmin and ascorbate oxidase but not in nitrite reductase, and therefore are considered to retain the characteristics of the plausible ancestral form of ceruloplasmin and ascorbate oxidase. A possible evolutionary relationship of these proteins is proposed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Ascorbate Oxidase / chemistry
  • Ascorbate Oxidase / genetics
  • Binding Sites
  • Ceruloplasmin / chemistry
  • Ceruloplasmin / genetics
  • Conserved Sequence
  • Copper / chemistry
  • Copper / metabolism
  • Evolution, Molecular*
  • Molecular Sequence Data
  • Nitrite Reductases / chemistry
  • Nitrite Reductases / genetics
  • Oxidoreductases / chemistry*
  • Oxidoreductases / genetics*
  • Oxidoreductases / metabolism
  • Phylogeny
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Copper
  • Oxidoreductases
  • Ascorbate Oxidase
  • copper oxidase
  • Ceruloplasmin
  • Nitrite Reductases