The primary structure of iron superoxide dismutase from Escherichia coli

• Published in: FEBS letters Vol. 221; no. 1; pp. 87 - 90
• Main Authors: Schininà, M.Eugenia, Maffey, Letizia, Barra, Donatella, Bossa, Francesco, Puget, Krystyna, Michelson, Adolf M.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 31.08.1987; Elsevier
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Cyanogen Bromide; Enzymes and enzyme inhibitors; Escherichia coli; Escherichia coli - enzymology; Fundamental and applied biological sciences. Psychology; Iron; Iron superoxide dismutase; Isoenzymes; Magnesium; Oxidoreductases; Peptide Fragments; Primary structure; Sequence homology; Superoxide Dismutase; Trypsin; Iron superoxide dismutase; Primary structure; Sequence homology; Enzyme; Escherichia coli; Bacteria; Superoxide dismutase; Escherichieae; Enterobacteriaceae
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(87)80357-5

The complete amino acid sequence of iron superoxide from Escherichia coli has been determined. The sequence was deduced from analysis of peptides obtained after cleavage of the carboxymethylated apoenzyme with trypsin, Stapholococcus aureus protease or CNBr. The polypeptide chain is made up of 192 residues and is easily aligned with the other known amino acid sequences of iron and manganese superoxide dismutases from various sources. The iron superoxide dismutase from E. coli shows a significantly higher homology with the iron enzyme from a different organism than with the manganese isoenzyme from E. coli.