The amino-acid sequence of copper/zinc superoxide dismutase from swordfish liver. Comparison of copper/zinc superoxide dismutase sequences

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Abstract
The amino acid sequence of Cu/Zn superoxide dismutase [EC 1.15.1.1] from swordfish (X. gladius) liver was determined by alignment of the tryptic peptides according to the known sequence of bovine erythrocyte Cu/Zn superoxide dismutase. This alignment resulted in the ligands to the Cu (His-47, 49, 76 and 94) and the Zn (His-76, 85, 134 and Asp-97) being conserved in all the Cu/Zn superoxide dismutases sequenced so far. Also conserved in the sequences were the cysteines forming the intrachain disulfide bridge (Cys-58 and 160) and the essential arginine (Arg-157). Comparison of the amino acid sequence of swordfish liver Cu/Zn superoxide dismutase with the bovine, human, horse, yeast and Photobacterium leiognathi indicated that the swordfish enzyme had a high homology with the other eukaryotic enzymes. Low homology was observed with the P. leiognathi enzyme.