A protein isolated from Brucella abortus is a Cu-Zn superoxide dismutase

Biochemistry. 1990 Jan 16;29(2):372-6. doi: 10.1021/bi00454a010.


Brucella abortus contains a protein that elicits an antigenic response in cattle previously exposed to the organism. The amino acid sequence of the recombinant form of this antigenic protein was determined by gas-phase sequencing of the pyridylethylated protein and its peptides obtained by digestion with cyanogen bromide (CNBr), clostripain, and Staphylococcus aureus V8 protease. The Brucella protein demonstrated 53.6% identity with the Cu-Zn superoxide dismutase (SOD) from Photobacterium leiognathi. Residues essential for metal coordination and enzymatic activity and cysteines required for the formation of the intrasubunit disulfide bridge of Cu-Zn SOD were conserved in the Brucella protein. also exhibited SOD activity that was inhibited by cyanide, which is characteristic of a Cu-Zn SOD. Brucella abortus Cu-Zn SOD is the second prokaryotic Cu-Zn SOD to be sequenced, and the fifth found in prokaryotes. The high degree of conservation between Photobacterium and Brucella Cu-Zn SOD supports the hypothesis of a separately evolved prokaryotic and eukaryotic Cu-Zn SOD gene.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Brucella abortus / enzymology*
  • Cyanogen Bromide
  • Cysteine Endopeptidases
  • Molecular Sequence Data
  • Peptide Fragments
  • Sequence Homology, Nucleic Acid
  • Serine Endopeptidases
  • Superoxide Dismutase / antagonists & inhibitors
  • Superoxide Dismutase / isolation & purification*


  • Amino Acids
  • Peptide Fragments
  • Superoxide Dismutase
  • Serine Endopeptidases
  • glutamyl endopeptidase
  • Cysteine Endopeptidases
  • clostripain
  • Cyanogen Bromide