Primary structure of copper-zinc superoxide dismutase from Neurospora crassa.

摘要: The complete amino acid sequence of copper-zinc superoxide dismutase from Neurospora crassa is reported. subunit consists 153 acids and has a Mr 15,850. primary structure was determined by automated manual analysis peptides obtained digestions the carboxymethylated aminoethylated enzyme with trypsin thermolysin. protein devoid tryptophan methionine displays free terminus. Comparison those human erythrocyte, bovine horse liver, swordfish yeast dismutases reveals high degree homology among six enzymes. Most prominently, regions containing residues participating in metal-binding half-cystine forming intramolecular disulfide bridge are highly conserved. invariant Pro 74 Asp 76 four vertebrate were found to be substituted arginine alanine, respectively, enzyme. These radical substitutions occurring zinc ligand region, known form characteristic loop erythrocyte (Tainer, J. A., Getzoff, E. D., Beem, K. M., Richardson, S., D. C. (1982) Mol. Biol. 160, 181-217), however, do not affect catalytic properties